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Chloroplast DNA
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<h2 id="molecular-structure">Molecular structure</h2> <p><a href="/facts/Chloroplast/fo8U3yTx">Chloroplast</a> DNAs are circular, and are typically 120,000–170,000 <a href="/facts/Base_pairs/xmPpPQ9W">base pairs</a> long.<a class="footnote-ref" id="fnref:7" href="#fn:7"><sup>7</sup></a><a class="footnote-ref" id="fnref:8" href="#fn:8"><sup>8</sup></a><a class="footnote-ref" id="fnref:9" href="#fn:9"><sup>9</sup></a> They can have a contour length of around 30–60 micrometers, and have a mass of about 80–130 million <a href="/facts/Dalton_(unit)/IMATU3vf">daltons</a>.<a class="footnote-ref" id="fnref:10" href="#fn:10"><sup>10</sup></a> </p><p>Most chloroplasts have their entire chloroplast genome combined into a single large ring, though those of <a href="/facts/Dinophyte_algae/jcQuSgM3">dinophyte algae</a> are a notable exception—their genome is broken up into about forty small <a href="/facts/Plasmids/yf59JVlA">plasmids</a>, each 2,000–10,000 <a href="/facts/Base_pairs/xmPpPQ9W">base pairs</a> long.<a class="footnote-ref" id="fnref:11" href="#fn:11"><sup>11</sup></a> Each minicircle contains one to three genes,<a class="footnote-ref" id="fnref:12" href="#fn:12"><sup>12</sup></a> but blank plasmids, with no <a href="/facts/Coding_DNA/eSR9aIKr">coding DNA</a>, have also been found. </p><p>Chloroplast DNA has long been thought to have a circular structure, but some evidence suggests that chloroplast DNA more commonly takes a linear shape.<a class="footnote-ref" id="fnref:13" href="#fn:13"><sup>13</sup></a> Over 95% of the chloroplast DNA in <a href="/facts/Corn/lJ6c5xMH">corn</a> chloroplasts has been observed to be in branched linear form rather than individual circles.<a class="footnote-ref" id="fnref:14" href="#fn:14"><sup>14</sup></a> </p> <h3>Inverted repeats</h3> <p>Many chloroplast DNAs contain two <i>inverted repeats</i>, which separate a long single copy section (LSC) from a short single copy section (SSC).<a class="footnote-ref" id="fnref:15" href="#fn:15"><sup>15</sup></a> </p><p>The inverted repeats vary wildly in length, ranging from 4,000 to 25,000 <a href="/facts/Base_pairs/xmPpPQ9W">base pairs</a> long each.<a class="footnote-ref" id="fnref:16" href="#fn:16"><sup>16</sup></a> Inverted repeats in plants tend to be at the upper end of this range, each being 20,000–25,000 base pairs long.<a class="footnote-ref" id="fnref:17" href="#fn:17"><sup>17</sup></a><a class="footnote-ref" id="fnref:18" href="#fn:18"><sup>18</sup></a> The inverted repeat regions usually contain three <a href="/facts/Ribosomal_RNA/zy5FxddY">ribosomal RNA</a> and two <a href="/facts/TRNA/pR9T5XSl">tRNA</a> genes, but they can be expanded or <a href="/facts/Genome_reduction/m30NcTL2">reduced</a> to contain as few as four or as many as over 150 genes.<a class="footnote-ref" id="fnref:19" href="#fn:19"><sup>19</sup></a> While a given pair of inverted repeats are rarely completely identical, they are always very similar to each other, apparently resulting from <a href="/facts/Concerted_evolution/gGQzVzJz">concerted evolution</a>.<a class="footnote-ref" id="fnref:20" href="#fn:20"><sup>20</sup></a> </p><p>The inverted repeat regions are highly <a href="/facts/Conserved_sequence/YAxy2Xa2">conserved</a> among land plants, and accumulate few mutations.<a class="footnote-ref" id="fnref:21" href="#fn:21"><sup>21</sup></a><a class="footnote-ref" id="fnref:22" href="#fn:22"><sup>22</sup></a> Similar inverted repeats exist in the genomes of cyanobacteria and the other two chloroplast lineages (<a href="/facts/Glaucophyta/gTuqKfI3">glaucophyta</a> and <a href="/facts/Red_algae/jCeIc7Kq">rhodophyceæ</a>), suggesting that they predate the chloroplast,<a class="footnote-ref" id="fnref:23" href="#fn:23"><sup>23</sup></a> though some chloroplast DNAs like those of <a href="/facts/Peas/hlndxpId">peas</a> and a few <a href="/facts/Red_algae/jCeIc7Kq">red algae</a><a class="footnote-ref" id="fnref:24" href="#fn:24"><sup>24</sup></a> have since lost the inverted repeats.<a class="footnote-ref" id="fnref:25" href="#fn:25"><sup>25</sup></a><a class="footnote-ref" id="fnref:26" href="#fn:26"><sup>26</sup></a> Others, like the red alga <i><a href="/facts/Porphyra/okXtms4p">Porphyra</a></i> flipped one of its inverted repeats (making them direct repeats).<a class="footnote-ref" id="fnref:27" href="#fn:27"><sup>27</sup></a> It is possible that the inverted repeats help stabilize the rest of the chloroplast genome, as chloroplast DNAs which have lost some of the inverted repeat segments tend to get rearranged more.<a class="footnote-ref" id="fnref:28" href="#fn:28"><sup>28</sup></a> </p> <h3>Nucleoids</h3> <p>Each chloroplast contains around 100 copies of its DNA in young leaves, declining to 15–20 copies in older leaves.<a class="footnote-ref" id="fnref:29" href="#fn:29"><sup>29</sup></a> They are usually packed into <a href="/facts/Nucleoids/nVJNKJDS">nucleoids</a> which can contain several identical chloroplast DNA rings. Many nucleoids can be found in each chloroplast.<a class="footnote-ref" id="fnref:30" href="#fn:30"><sup>30</sup></a> </p><p>Though chloroplast DNA is not associated with true <a href="/facts/Histone/krb5VJfp">histones</a>,<a class="footnote-ref" id="fnref:31" href="#fn:31"><sup>31</sup></a> in <a href="/facts/Red_algae/jCeIc7Kq">red algae</a>, a histone-like chloroplast protein (HC) coded by the chloroplast DNA that tightly packs each chloroplast DNA ring into a <a href="/facts/Nucleoid/nVJNKJDS">nucleoid</a> has been found.<a class="footnote-ref" id="fnref:32" href="#fn:32"><sup>32</sup></a> </p><p>In primitive <a href="/facts/Red_algae/jCeIc7Kq">red algae</a>, the chloroplast DNA nucleoids are clustered in the center of a chloroplast, while in green plants and <a href="/facts/Green_algae/3NlQ6pKF">green algae</a>, the nucleoids are dispersed throughout the <a href="/facts/Stroma_(fluid)/AYwQHKSm">stroma</a>.<a class="footnote-ref" id="fnref:33" href="#fn:33"><sup>33</sup></a> </p> <h2 id="gene-content-and-plastid-gene-expression">Gene content and plastid gene expression</h2> <p class="note">See also: <a href="/facts/List_of_sequenced_plastomes/QyAxTbQm">List of sequenced plastomes</a></p> <p>More than 5000 chloroplast genomes have been <a href="/facts/DNA_sequencing/hsPsNCQW">sequenced</a> and are accessible via the NCBI organelle genome database.<a class="footnote-ref" id="fnref:34" href="#fn:34"><sup>34</sup></a> The first chloroplast genomes were sequenced in 1986, from tobacco (<i>Nicotiana tabacum</i>)<a class="footnote-ref" id="fnref:35" href="#fn:35"><sup>35</sup></a> and liverwort (<i>Marchantia polymorpha</i>).<a class="footnote-ref" id="fnref:36" href="#fn:36"><sup>36</sup></a> Comparison of the gene sequences of the cyanobacteria <i>Synechocystis</i> to those of the chloroplast genome of <i>Arabidopsis</i> provided confirmation of the <a href="/facts/Endosymbiont/eWvSS8ID">endosymbiotic</a> origin of the chloroplast.<a class="footnote-ref" id="fnref:37" href="#fn:37"><sup>37</sup></a><a class="footnote-ref" id="fnref:38" href="#fn:38"><sup>38</sup></a> It also demonstrated the significant extent of <a href="/facts/Horizontal_gene_transfer/FPyUIsf2">gene transfer</a> from the cyanobacterial ancestor to the nuclear genome. </p><p>In most plant species, the chloroplast genome encodes approximately 120 genes.<a class="footnote-ref" id="fnref:39" href="#fn:39"><sup>39</sup></a><a class="footnote-ref" id="fnref:40" href="#fn:40"><sup>40</sup></a> The genes primarily encode core components of the photosynthetic machinery and factors involved in their expression and assembly.<a class="footnote-ref" id="fnref:41" href="#fn:41"><sup>41</sup></a> Across species of land plants, the set of genes encoded by the chloroplast genome is fairly conserved. This includes four <a href="/facts/Ribosomal_RNAs/zy5FxddY">ribosomal RNAs</a>, approximately 30 <a href="/facts/TRNAs/pR9T5XSl">tRNAs</a>, 21 <a href="/facts/Ribosomal_proteins/73JJEmgN">ribosomal proteins</a>, and 4 subunits of the plastid-encoded <a href="/facts/RNA_polymerase/gHd0ET9R">RNA polymerase</a> complex that are involved in plastid gene expression.<a class="footnote-ref" id="fnref:42" href="#fn:42"><sup>42</sup></a> The large <a href="/facts/Rubisco/C8asuQsc">Rubisco</a> subunit and 28 photosynthetic <a href="/facts/Thylakoid/d9PEe649">thylakoid</a> proteins are encoded within the chloroplast genome.<a class="footnote-ref" id="fnref:43" href="#fn:43"><sup>43</sup></a> </p> <h3>Chloroplast genome reduction and gene transfer</h3> <p>Over time, many parts of the chloroplast genome were transferred to the <a href="/facts/Nuclear_genome/5wzCJQlb">nuclear genome</a> of the host,<a class="footnote-ref" id="fnref:44" href="#fn:44"><sup>44</sup></a><a class="footnote-ref" id="fnref:45" href="#fn:45"><sup>45</sup></a><a class="footnote-ref" id="fnref:46" href="#fn:46"><sup>46</sup></a> a process called <i><a href="/facts/Endosymbiotic_gene_transfer/x2oEcP1P">endosymbiotic gene transfer</a></i>. As a result, the chloroplast genome is heavily <a href="/facts/Genome_reduction/m30NcTL2">reduced</a> compared to that of free-living cyanobacteria. Chloroplasts may contain 60–100 genes whereas cyanobacteria often have more than 1500 genes in their genome.<a class="footnote-ref" id="fnref:47" href="#fn:47"><sup>47</sup></a> The parasitic <i><a href="/facts/Pilostyles/PSUeH34x">Pilostyles</a></i> have even lost their plastid genes for <a href="/facts/TRNA/pR9T5XSl">tRNA</a>.<a class="footnote-ref" id="fnref:48" href="#fn:48"><sup>48</sup></a> Contrarily, there are only a few known instances where genes have been transferred to the chloroplast from various donors, including bacteria.<a class="footnote-ref" id="fnref:49" href="#fn:49"><sup>49</sup></a><a class="footnote-ref" id="fnref:50" href="#fn:50"><sup>50</sup></a><a class="footnote-ref" id="fnref:51" href="#fn:51"><sup>51</sup></a> </p><p>Endosymbiotic gene transfer is how we know about the <a href="/facts/Chloroplast/fo8U3yTx">lost chloroplasts</a> in many <a href="/facts/Chromalveolate/a13nzwd7">chromalveolate</a> lineages. Even if a chloroplast is eventually lost, the genes it donated to the former host's nucleus persist, providing evidence for the lost chloroplast's existence. For example, while <a href="/facts/Diatoms/x2oEcP1P">diatoms</a> (a <a href="/facts/Heterokontophyte/WFevSvg2">heterokontophyte</a>) now have a <a href="/facts/Red_algal_derived_chloroplast/fo8U3yTx">red algal derived chloroplast</a>, the presence of many <a href="/facts/Green_algal/3NlQ6pKF">green algal</a> genes in the diatom nucleus provide evidence that the diatom ancestor (probably the ancestor of all chromalveolates too) had a <a href="/facts/Green_algal_derived_chloroplast/fo8U3yTx">green algal derived chloroplast</a> at some point, which was subsequently replaced by the red chloroplast.<a class="footnote-ref" id="fnref:52" href="#fn:52"><sup>52</sup></a> </p><p>In land plants, some 11–14% of the DNA in their nuclei can be traced back to the chloroplast,<a class="footnote-ref" id="fnref:53" href="#fn:53"><sup>53</sup></a> up to 18% in <i><a href="/facts/Arabidopsis/SCz1CG26">Arabidopsis</a></i>, corresponding to about 4,500 protein-coding genes.<a class="footnote-ref" id="fnref:54" href="#fn:54"><sup>54</sup></a> There have been a few recent transfers of genes from the chloroplast DNA to the nuclear genome in land plants.<a class="footnote-ref" id="fnref:55" href="#fn:55"><sup>55</sup></a> </p> <h3>Proteins encoded by the chloroplast</h3> <p>Of the approximately three-thousand proteins found in chloroplasts, some 95% of them are encoded by nuclear genes. Many of the chloroplast's protein complexes consist of subunits from both the chloroplast genome and the host's nuclear genome. As a result, <a href="/facts/Protein_synthesis/P4IcGjPd">protein synthesis</a> must be coordinated between the chloroplast and the nucleus. The chloroplast is mostly under nuclear control, though chloroplasts can also give out signals regulating <a href="/facts/Gene_expression/alCPohLR">gene expression</a> in the nucleus, called <i><a href="/facts/Retrograde_signaling_(cell_biology)/tuSHb1Pj">retrograde signaling</a></i>.<a class="footnote-ref" id="fnref:56" href="#fn:56"><sup>56</sup></a> </p> <h3>Protein synthesis</h3> <p class="note">See also: <a href="/facts/Transcription_(genetics)/bDgp9HDN">Transcription</a> and <a href="/facts/Translation_(biology)/JcPC1rth">translation</a></p> <p>Protein synthesis within chloroplasts relies on an <a href="/facts/RNA_polymerase/gHd0ET9R">RNA polymerase</a> coded by the chloroplast's own genome, which is related to RNA polymerases found in bacteria. Chloroplasts also contain a mysterious second RNA polymerase that is encoded by the plant's nuclear genome. The two RNA polymerases may recognize and bind to different kinds of <a href="/facts/Promoter_(genetics)/YDYBzLfg">promoters</a> within the chloroplast genome.<a class="footnote-ref" id="fnref:57" href="#fn:57"><sup>57</sup></a> The <a href="/facts/Ribosome/CF2u2gtg">ribosomes</a> in chloroplasts are similar to bacterial ribosomes.<a class="footnote-ref" id="fnref:58" href="#fn:58"><sup>58</sup></a> </p> <h3>RNA editing in plastids</h3> <p><a href="/facts/RNA_editing/c2zGKWKo">RNA editing</a> is the insertion, deletion, and substitution of nucleotides in a mRNA transcript prior to translation to protein. The highly oxidative environment inside chloroplasts increases the rate of mutation so post-transcription repairs are needed to conserve functional sequences. The chloroplast editosome substitutes C -> U and U -> C at very specific locations on the transcript. This can change the codon for an amino acid or restore a non-functional pseudogene by adding an AUG start codon or removing a premature UAA stop codon.<a class="footnote-ref" id="fnref:59" href="#fn:59"><sup>59</sup></a> </p><p>The editosome recognizes and binds to cis sequence upstream of the editing site. The distance between the binding site and editing site varies by gene and proteins involved in the editosome. Hundreds of different <a href="/facts/PPR_protein/7cVsWg95">PPR proteins</a> from the nuclear genome are involved in the RNA editing process. These proteins consist of 35-mer repeated amino acids, the sequence of which determines the cis binding site for the edited transcript.<a class="footnote-ref" id="fnref:60" href="#fn:60"><sup>60</sup></a> </p><p>Basal land plants such as liverworts, mosses and ferns have hundreds of different editing sites while flowering plants typically have between thirty and forty. Parasitic plants such as <a href="/facts/Epifagus_virginiana/UE61z5GA">Epifagus virginiana</a> show a loss of RNA editing resulting in a loss of function for photosynthesis genes.<a class="footnote-ref" id="fnref:61" href="#fn:61"><sup>61</sup></a> </p> <h2 id="dna-replication">DNA replication</h2> <h3>Leading model of cpDNA replication</h3> <p>The mechanism for chloroplast DNA (cpDNA) replication has not been conclusively determined, but two main models have been proposed. Scientists have attempted to observe chloroplast replication via <a href="/facts/Electron_microscopy/XtaBktwF">electron microscopy</a> since the 1970s.<a class="footnote-ref" id="fnref:62" href="#fn:62"><sup>62</sup></a><a class="footnote-ref" id="fnref:63" href="#fn:63"><sup>63</sup></a> The results of the microscopy experiments led to the idea that chloroplast DNA replicates using a double displacement loop (D-loop). As the <a href="/facts/D-loop/4yt3q9n9">D-loop</a> moves through the circular DNA, it adopts a theta intermediary form, also known as a Cairns replication intermediate, and completes replication with a rolling circle mechanism.<a class="footnote-ref" id="fnref:64" href="#fn:64"><sup>64</sup></a><a class="footnote-ref" id="fnref:65" href="#fn:65"><sup>65</sup></a> Replication starts at specific points of origin. Multiple <a href="/facts/Replication_fork/wrU6RuR3">replication forks</a> open up, allowing replication machinery to replicate the DNA. As replication continues, the forks grow and eventually converge. The new cpDNA structures separate, creating daughter cpDNA chromosomes. </p><p>In addition to the early microscopy experiments, this model is also supported by the amounts of <a href="/facts/Deamination/aBIhMC23">deamination</a> seen in cpDNA.<a class="footnote-ref" id="fnref:66" href="#fn:66"><sup>66</sup></a> Deamination occurs when an <a href="/facts/Amino_group/SN7W44fv">amino group</a> is lost and is a <a href="/facts/Mutation/Ee4NnWbY">mutation</a> that often results in base changes. When adenine is deaminated, it becomes <a href="/facts/Hypoxanthine/QIyA0sQr">hypoxanthine</a> (H). Hypoxanthine can bind to <a href="/facts/Cytosine/JW20j33u">cytosine</a>, and when the HC base pair is replicated, it becomes a GC (thus, an A → G base change).<a class="footnote-ref" id="fnref:67" href="#fn:67"><sup>67</sup></a> </p> <p>In cpDNA, there are several A → G deamination gradients. DNA becomes susceptible to deamination events when it is single stranded. When replication forks form, the strand not being copied is single stranded, and thus at risk for A → G deamination. Therefore, gradients in deamination indicate that replication forks were most likely present and the direction that they initially opened (the highest gradient is most likely nearest the start site because it was single stranded for the longest amount of time).<a class="footnote-ref" id="fnref:68" href="#fn:68"><sup>68</sup></a> This mechanism is still the leading theory today; however, a second theory suggests that most cpDNA is actually linear and replicates through homologous recombination. It further contends that only a minority of the genetic material is kept in circular chromosomes while the rest is in branched, linear, or other complex structures.<a class="footnote-ref" id="fnref:69" href="#fn:69"><sup>69</sup></a><a class="footnote-ref" id="fnref:70" href="#fn:70"><sup>70</sup></a> </p> <h3>Alternative model of replication</h3> <p>One of the main competing models for cpDNA asserts that most cpDNA is linear and participates in <a href="/facts/Homologous_recombination/WU0IIVVv">homologous recombination</a> and replication structures similar to <a href="/facts/Bacteriophage_T4/Af4UyJxy">bacteriophage T4</a>.<a class="footnote-ref" id="fnref:71" href="#fn:71"><sup>71</sup></a> It has been established that some plants have linear cpDNA, such as maize, and that more still contain complex structures that scientists do not yet understand;<a class="footnote-ref" id="fnref:72" href="#fn:72"><sup>72</sup></a> however, the predominant view today is that most cpDNA is circular. When the original experiments on cpDNA were performed, scientists did notice linear structures; however, they attributed these linear forms to broken circles.<a class="footnote-ref" id="fnref:73" href="#fn:73"><sup>73</sup></a> If the branched and complex structures seen in cpDNA experiments are real and not artifacts of concatenated circular DNA or broken circles, then a D-loop mechanism of replication is insufficient to explain how those structures would replicate.<a class="footnote-ref" id="fnref:74" href="#fn:74"><sup>74</sup></a> At the same time, homologous recombination does not explain the multiple A → G gradients seen in plastomes.<a class="footnote-ref" id="fnref:75" href="#fn:75"><sup>75</sup></a> This shortcoming is one of the biggest for the linear structure theory. </p> <h2 id="protein-targeting-and-import">Protein targeting and import</h2> <p class="note">See also: <a href="/facts/Protein_targeting/R3B37xMM">Protein targeting</a></p> <p>The movement of so many chloroplast genes to the nucleus means that many chloroplast <a href="/facts/Proteins/Jxmagu3E">proteins</a> that were supposed to be <a href="/facts/Translation_(biology)/JcPC1rth">translated</a> in the chloroplast are now synthesized in the cytoplasm. This means that these proteins must be directed back to the chloroplast, and imported through at least two chloroplast membranes.<a class="footnote-ref" id="fnref:76" href="#fn:76"><sup>76</sup></a> </p><p>Curiously, around half of the protein products of transferred genes aren't even targeted back to the chloroplast. Many became <a href="/facts/Exaptations/aK8nu0xE">exaptations</a>, taking on new functions like participating in <a href="/facts/Cell_division/n5MrunWj">cell division</a>, <a href="/facts/Protein_routing/R3B37xMM">protein routing</a>, and even <a href="/facts/Disease_resistance/6lxBUjoh">disease resistance</a>. A few chloroplast genes found new homes in the <a href="/facts/Mitochondrial_genome/goC0ex0X">mitochondrial genome</a>—most became nonfunctional <a href="/facts/Pseudogenes/VfbL4L07">pseudogenes</a>, though a few <a href="/facts/TRNA/pR9T5XSl">tRNA</a> genes still work in the <a href="/facts/Mitochondrion/ErHqrdJ1">mitochondrion</a>.<a class="footnote-ref" id="fnref:77" href="#fn:77"><sup>77</sup></a> Some transferred chloroplast DNA protein products get directed to the <a href="/facts/Secretory_pathway/VHk9eLAV">secretory pathway</a><a class="footnote-ref" id="fnref:78" href="#fn:78"><sup>78</sup></a> (though many <a href="/facts/Secondary_plastids/fo8U3yTx">secondary plastids</a> are bounded by an outermost membrane derived from the host's <a href="/facts/Cell_membrane/vAXSD0DT">cell membrane</a>, and therefore <a href="/facts/Topologically/2EqW47cU">topologically</a> outside of the cell, because to reach the chloroplast from the <a href="/facts/Cytosol/VyXgygWm">cytosol</a>, you have to cross the <a href="/facts/Cell_membrane/vAXSD0DT">cell membrane</a>, just like if you were headed for the <a href="/facts/Extracellular_space/E1Vaq60Y">extracellular space</a>. In those cases, chloroplast-targeted proteins do initially travel along the secretory pathway).<a class="footnote-ref" id="fnref:79" href="#fn:79"><sup>79</sup></a> </p><p>Because the cell acquiring a chloroplast <a href="/facts/Chloroplast/fo8U3yTx">already</a> had <a href="/facts/Mitochondria/ErHqrdJ1">mitochondria</a> (and <a href="/facts/Peroxisomes/sEW1RBmb">peroxisomes</a>, and a <a href="/facts/Cell_membrane/vAXSD0DT">cell membrane</a> for secretion), the new chloroplast host had to develop a unique <a href="/facts/Protein_targeting_system/R3B37xMM">protein targeting system</a> to avoid having chloroplast proteins being sent to the wrong <a href="/facts/Organelle/vhDFnGbs">organelle</a>.<a class="footnote-ref" id="fnref:80" href="#fn:80"><sup>80</sup></a> </p> <h3>Cytoplasmic translation and N-terminal transit sequences</h3> <p class="note">See also: <a href="/facts/Polypeptide/C4ltc7UG">Polypeptide</a>, <a href="/facts/Protein/Jxmagu3E">protein</a>, and <a href="/facts/Translation_(biology)/JcPC1rth">translation</a></p> <p><a href="/facts/Polypeptides/C4ltc7UG">Polypeptides</a>, the precursors of <a href="/facts/Proteins/Jxmagu3E">proteins</a>, are chains of <a href="/facts/Amino_acids/WDxYwBny">amino acids</a>. The two ends of a polypeptide are called the <a href="/facts/N-terminus/yKYpuaBJ">N-terminus</a>, or <i>amino end</i>, and the <a href="/facts/C-terminus/ws4scHgT">C-terminus</a>, or <i>carboxyl end</i>.<a class="footnote-ref" id="fnref:81" href="#fn:81"><sup>81</sup></a> For many (but not all)<a class="footnote-ref" id="fnref:82" href="#fn:82"><sup>82</sup></a> chloroplast proteins encoded by <a href="/facts/Cell_nucleus/D7sFRa3c">nuclear</a> genes, <i><a href="/facts/Cleavable_transit_peptides/9oARjq52">cleavable transit peptides</a></i> are added to the N-termini of the polypeptides, which are used to help direct the polypeptide to the chloroplast for import<a class="footnote-ref" id="fnref:83" href="#fn:83"><sup>83</sup></a><a class="footnote-ref" id="fnref:84" href="#fn:84"><sup>84</sup></a> (N-terminal transit peptides are also used to direct polypeptides to plant <a href="/facts/Mitochondria/ErHqrdJ1">mitochondria</a>).<a class="footnote-ref" id="fnref:85" href="#fn:85"><sup>85</sup></a> N-terminal transit sequences are also called <i>presequences</i><a class="footnote-ref" id="fnref:86" href="#fn:86"><sup>86</sup></a> because they are located at the "front" end of a polypeptide—<a href="/facts/Ribosomes/CF2u2gtg">ribosomes</a> synthesize polypeptides from the N-terminus to the C-terminus.<a class="footnote-ref" id="fnref:87" href="#fn:87"><sup>87</sup></a> </p><p>Chloroplast transit peptides exhibit huge variation in length and <a href="/facts/Amino_acid_sequence/QNBoERdu">amino acid sequence</a>.<a class="footnote-ref" id="fnref:88" href="#fn:88"><sup>88</sup></a> They can be from 20 to 150 amino acids long<a class="footnote-ref" id="fnref:89" href="#fn:89"><sup>89</sup></a>—an unusually long length, suggesting that transit peptides are actually collections of <a href="/facts/Protein_domain/oUpFcSsl">domains</a> with different functions.<a class="footnote-ref" id="fnref:90" href="#fn:90"><sup>90</sup></a> Transit peptides tend to be <a href="/facts/Positively_charged/xxsBfmlB">positively charged</a>,<a class="footnote-ref" id="fnref:91" href="#fn:91"><sup>91</sup></a> rich in <a href="/facts/Hydroxyl_group/1Hs2QAEv">hydroxylated</a> amino acids such as <a href="/facts/Serine/4duVl30B">serine</a>, <a href="/facts/Threonine/7zffFQ6W">threonine</a>, and <a href="/facts/Proline/x1ABSW5A">proline</a>, and poor in <a href="/facts/Acidic/FySU18n1">acidic</a> amino acids like <a href="/facts/Aspartic_acid/9DFSFPa1">aspartic acid</a> and <a href="/facts/Glutamic_acid/7oXbNcvu">glutamic acid</a>.<a class="footnote-ref" id="fnref:92" href="#fn:92"><sup>92</sup></a> In an <a href="/facts/Aqueous_solution/eRNr3MH2">aqueous solution</a>, the transit sequence forms a random coil.<a class="footnote-ref" id="fnref:93" href="#fn:93"><sup>93</sup></a> </p><p>Not all chloroplast proteins include a N-terminal cleavable transit peptide though.<a class="footnote-ref" id="fnref:94" href="#fn:94"><sup>94</sup></a> Some include the transit sequence within the <a href="/facts/Mature_protein/KMUayTIc">functional part</a> of the protein itself.<a class="footnote-ref" id="fnref:95" href="#fn:95"><sup>95</sup></a> A few have their transit sequence appended to their <a href="/facts/C-terminus/ws4scHgT">C-terminus</a> instead.<a class="footnote-ref" id="fnref:96" href="#fn:96"><sup>96</sup></a> Most of the polypeptides that lack N-terminal targeting sequences are the ones that are sent to the <a href="/facts/Outer_chloroplast_membrane/JefvL8Dp">outer chloroplast membrane</a>, plus at least one sent to the <a href="/facts/Inner_chloroplast_membrane/JefvL8Dp">inner chloroplast membrane</a>.<a class="footnote-ref" id="fnref:97" href="#fn:97"><sup>97</sup></a> </p> <h3>Phosphorylation, chaperones, and transport</h3> <p>After a chloroplast <a href="/facts/Polypeptide/C4ltc7UG">polypeptide</a> is synthesized on a <a href="/facts/Ribosome/CF2u2gtg">ribosome</a> in the <a href="/facts/Cytosol/VyXgygWm">cytosol</a>, <a href="/facts/Adenosine_triphosphate/nB9bwgcU">ATP</a> energy can be used to <a href="/facts/Phosphorylate/LXUEEeIL">phosphorylate</a>, or add a <a href="/facts/Phosphate_group/FDGVCxUG">phosphate group</a> to many (but not all) of them in their transit sequences.<a class="footnote-ref" id="fnref:98" href="#fn:98"><sup>98</sup></a> <a href="/facts/Serine/4duVl30B">Serine</a> and <a href="/facts/Threonine/7zffFQ6W">threonine</a> (both very common in chloroplast transit sequences—making up 20–30% of the sequence)<a class="footnote-ref" id="fnref:99" href="#fn:99"><sup>99</sup></a> are often the <a href="/facts/Amino_acids/WDxYwBny">amino acids</a> that accept the <a href="/facts/Phosphate_group/FDGVCxUG">phosphate group</a>.<a class="footnote-ref" id="fnref:100" href="#fn:100"><sup>100</sup></a><a class="footnote-ref" id="fnref:101" href="#fn:101"><sup>101</sup></a> The <a href="/facts/Protein_kinase/U4DQVhW3">enzyme</a> that carries out the phosphorylation is <a href="/facts/Enzyme_specificity/zAzbLh09">specific</a> for chloroplast polypeptides, and ignores ones meant for <a href="/facts/Mitochondria/ErHqrdJ1">mitochondria</a> or <a href="/facts/Peroxisomes/sEW1RBmb">peroxisomes</a>.<a class="footnote-ref" id="fnref:102" href="#fn:102"><sup>102</sup></a> </p><p>Phosphorylation changes the polypeptide's shape,<a class="footnote-ref" id="fnref:103" href="#fn:103"><sup>103</sup></a> making it easier for <a href="/facts/14-3-3_proteins/260dE39l">14-3-3 proteins</a> to attach to the polypeptide.<a class="footnote-ref" id="fnref:104" href="#fn:104"><sup>104</sup></a><a class="footnote-ref" id="fnref:105" href="#fn:105"><sup>105</sup></a> In plants, <a href="/facts/14-3-3_proteins/260dE39l">14-3-3 proteins</a> only bind to chloroplast preproteins.<a class="footnote-ref" id="fnref:106" href="#fn:106"><sup>106</sup></a> It is also bound by the <a href="/facts/Heat_shock_protein/PxDzSx0g">heat shock protein</a> <a href="/facts/Hsp70/Knm5v3Yv">Hsp70</a> that keeps the polypeptide from <a href="/facts/Protein_folding/rf3nR2Y1">folding</a> prematurely.<a class="footnote-ref" id="fnref:107" href="#fn:107"><sup>107</sup></a> This is important because it prevents chloroplast proteins from assuming their active form and carrying out their chloroplast functions in the wrong place—the <a href="/facts/Cytosol/VyXgygWm">cytosol</a>.<a class="footnote-ref" id="fnref:108" href="#fn:108"><sup>108</sup></a><a class="footnote-ref" id="fnref:109" href="#fn:109"><sup>109</sup></a> At the same time, they have to keep just enough shape so that they can be recognized and imported into the chloroplast.<a class="footnote-ref" id="fnref:110" href="#fn:110"><sup>110</sup></a> </p><p>The heat shock protein and the 14-3-3 proteins together form a cytosolic guidance complex that makes it easier for the chloroplast polypeptide to get imported into the chloroplast.<a class="footnote-ref" id="fnref:111" href="#fn:111"><sup>111</sup></a> </p><p>Alternatively, if a chloroplast preprotein's transit peptide is not phosphorylated, a chloroplast preprotein can still attach to a heat shock protein or Toc159. These complexes can bind to the <a href="/facts/TOC_complex/WPWPSS6E">TOC complex</a> on the outer chloroplast membrane using <a href="/facts/Guanosine_triphosphate/NAwoHjTW">GTP</a> energy.<a class="footnote-ref" id="fnref:112" href="#fn:112"><sup>112</sup></a> </p> <h3>The translocon on the outer chloroplast membrane (TOC)</h3> <p>The <a href="/facts/TOC_complex/WPWPSS6E">TOC complex</a>, or <i><a href="/facts/Translocon/qfPhCvM5">translocon</a> on the outer chloroplast membrane</i>, is a collection of proteins that imports preproteins across the <a href="/facts/Outer_chloroplast_envelope/JefvL8Dp">outer chloroplast envelope</a>. Five <a href="/facts/Protein_subunit/HhuET9UP">subunits</a> of the TOC complex have been identified—two <a href="/facts/Guanosine_triphosphate/NAwoHjTW">GTP</a>-binding proteins Toc34 and Toc159, the protein import tunnel Toc75, plus the proteins Toc64<a class="footnote-ref" id="fnref:113" href="#fn:113"><sup>113</sup></a> and Toc12.<a class="footnote-ref" id="fnref:114" href="#fn:114"><sup>114</sup></a> </p><p>The first three proteins form a core complex that consists of one Toc159, four to five Toc34s, and four Toc75s that form four holes in a disk 13 <a href="/facts/Nanometers/a98sjHyu">nanometers</a> across. The whole core complex weighs about 500 <a href="/facts/Kilodaltons/IMATU3vf">kilodaltons</a>. The other two proteins, Toc64 and Toc12, are associated with the core complex but are not part of it.<a class="footnote-ref" id="fnref:115" href="#fn:115"><sup>115</sup></a> </p> <h4>Toc34 and 33</h4> <p>Toc34 is an <a href="/facts/Integral_protein/Vztpmlu1">integral protein</a> in the outer chloroplast membrane that's anchored into it by its <a href="/facts/Hydrophobic/Ifya0CXQ">hydrophobic</a><a class="footnote-ref" id="fnref:116" href="#fn:116"><sup>116</sup></a> <a href="/facts/C-terminal/ws4scHgT">C-terminal</a> tail.<a class="footnote-ref" id="fnref:117" href="#fn:117"><sup>117</sup></a><a class="footnote-ref" id="fnref:118" href="#fn:118"><sup>118</sup></a> Most of the protein, however, including its large <a href="/facts/Guanosine_triphosphate/NAwoHjTW">guanosine triphosphate</a> (GTP)-binding <a href="/facts/Protein_domain/oUpFcSsl">domain</a> projects out into the stroma.<a class="footnote-ref" id="fnref:119" href="#fn:119"><sup>119</sup></a> </p><p>Toc34's job is to catch some chloroplast <a href="/facts/Preproteins/A1vxb5mN">preproteins</a> in the <a href="/facts/Cytosol/VyXgygWm">cytosol</a> and hand them off to the rest of the TOC complex.<a class="footnote-ref" id="fnref:120" href="#fn:120"><sup>120</sup></a> When <a href="/facts/Guanosine_triphosphate/NAwoHjTW">GTP</a>, an energy molecule similar to <a href="/facts/Adenosine_triphosphate/nB9bwgcU">ATP</a> attaches to Toc34, the protein becomes much more able to bind to many chloroplast preproteins in the <a href="/facts/Cytosol/VyXgygWm">cytosol</a>.<a class="footnote-ref" id="fnref:121" href="#fn:121"><sup>121</sup></a> The chloroplast preprotein's presence causes Toc34 to break GTP into <a href="/facts/Guanosine_diphosphate/3BkkMql3">guanosine diphosphate</a> (GDP) and <a href="/facts/Inorganic_phosphate/FDGVCxUG">inorganic phosphate</a>. This loss of GTP makes the Toc34 protein release the chloroplast preprotein, handing it off to the next TOC protein.<a class="footnote-ref" id="fnref:122" href="#fn:122"><sup>122</sup></a> Toc34 then releases the depleted GDP molecule, probably with the help of an unknown <a href="/facts/GDP_exchange_factor/0baXbBeM">GDP exchange factor</a>. A <a href="/facts/Protein_domain/oUpFcSsl">domain</a> of Toc159 might be the exchange factor that carry out the GDP removal. The Toc34 protein can then take up another molecule of GTP and begin the cycle again.<a class="footnote-ref" id="fnref:123" href="#fn:123"><sup>123</sup></a> </p><p>Toc34 can be turned off through <a href="/facts/Phosphorylation/LXUEEeIL">phosphorylation</a>. A <a href="/facts/Protein_kinase/U4DQVhW3">protein kinase</a> drifting around on the outer chloroplast membrane can use <a href="/facts/Adenosine_triphosphate/nB9bwgcU">ATP</a> to add a <a href="/facts/Phosphate_group/FDGVCxUG">phosphate group</a> to the Toc34 protein, preventing it from being able to receive another <a href="/facts/Guanosine_triphosphate/NAwoHjTW">GTP</a> molecule, inhibiting the protein's activity. This might provide a way to regulate protein import into chloroplasts.<a class="footnote-ref" id="fnref:124" href="#fn:124"><sup>124</sup></a><a class="footnote-ref" id="fnref:125" href="#fn:125"><sup>125</sup></a> </p><p><i><a href="/facts/Arabidopsis_thaliana/wt2IMJsC">Arabidopsis thaliana</a></i> has two <a href="/facts/Homologous_series/7PKCuvzm">homologous</a> proteins, AtToc33 and AtToc34 (The <i>At</i> stands for <i>Arabidopsis thaliana</i>),<a class="footnote-ref" id="fnref:126" href="#fn:126"><sup>126</sup></a><a class="footnote-ref" id="fnref:127" href="#fn:127"><sup>127</sup></a> which are each about 60% identical in <a href="/facts/Amino_acid_sequence/QNBoERdu">amino acid sequence</a> to Toc34 in <a href="/facts/Peas/hlndxpId">peas</a> (called <i>ps</i>Toc34).<a class="footnote-ref" id="fnref:128" href="#fn:128"><sup>128</sup></a> AtToc33 is the most common in <i>Arabidopsis</i>,<a class="footnote-ref" id="fnref:129" href="#fn:129"><sup>129</sup></a> and it is the functional <a href="/facts/Analogy_(biology)/dd0L8z4R">analogue</a> of Toc34 because it can be turned off by phosphorylation. AtToc34 on the other hand cannot be phosphorylated.<a class="footnote-ref" id="fnref:130" href="#fn:130"><sup>130</sup></a><a class="footnote-ref" id="fnref:131" href="#fn:131"><sup>131</sup></a> </p> <h4>Toc159</h4> <p>Toc159 is another <a href="/facts/Guanosine_triphosphate/NAwoHjTW">GTP</a> binding TOC <a href="/facts/Protein_subunit/HhuET9UP">subunit</a>, like Toc34. Toc159 has three <a href="/facts/Protein_domain/oUpFcSsl">domains</a>. At the <a href="/facts/N-terminal/yKYpuaBJ">N-terminal</a> end is the A-domain, which is rich in <a href="/facts/Acidic_amino_acids/PYbVToXJ">acidic amino acids</a> and takes up about half the protein length.<a class="footnote-ref" id="fnref:132" href="#fn:132"><sup>132</sup></a><a class="footnote-ref" id="fnref:133" href="#fn:133"><sup>133</sup></a> The A-domain is often <a href="/facts/Protein_cleavage/KMUayTIc">cleaved</a> off, leaving an 86 <a href="/facts/Kilodalton/IMATU3vf">kilodalton</a> fragment called Toc86.<a class="footnote-ref" id="fnref:134" href="#fn:134"><sup>134</sup></a> In the middle is its <a href="/facts/Guanosine_triphosphate/NAwoHjTW">GTP</a> binding domain, which is very similar to the <a href="/facts/Homology_(biology)/muctKlyT">homologous</a> GTP-binding domain in Toc34.<a class="footnote-ref" id="fnref:135" href="#fn:135"><sup>135</sup></a><a class="footnote-ref" id="fnref:136" href="#fn:136"><sup>136</sup></a> At the <a href="/facts/C-terminal/ws4scHgT">C-terminal</a> end is the <a href="/facts/Hydrophilic/k8p95WYu">hydrophilic</a> M-domain,<a class="footnote-ref" id="fnref:137" href="#fn:137"><sup>137</sup></a> which anchors the protein to the outer chloroplast membrane.<a class="footnote-ref" id="fnref:138" href="#fn:138"><sup>138</sup></a> </p><p>Toc159 probably works a lot like Toc34, recognizing proteins in the cytosol using <a href="/facts/Guanosine_triphosphate/NAwoHjTW">GTP</a>. It can be regulated through <a href="/facts/Phosphorylation/LXUEEeIL">phosphorylation</a>, but by a different <a href="/facts/Protein_kinase/U4DQVhW3">protein kinase</a> than the one that phosphorylates Toc34.<a class="footnote-ref" id="fnref:139" href="#fn:139"><sup>139</sup></a> Its M-domain forms part of the tunnel that chloroplast preproteins travel through, and seems to provide the force that pushes preproteins through, using the energy from <a href="/facts/Guanosine_triphosphate/NAwoHjTW">GTP</a>.<a class="footnote-ref" id="fnref:140" href="#fn:140"><sup>140</sup></a> </p><p>Toc159 is not always found as part of the TOC complex—it has also been found dissolved in the <a href="/facts/Cytosol/VyXgygWm">cytosol</a>. This suggests that it might act as a shuttle that finds chloroplast preproteins in the cytosol and carries them back to the TOC complex. There isn't a lot of direct evidence for this behavior though.<a class="footnote-ref" id="fnref:141" href="#fn:141"><sup>141</sup></a> </p><p>A family of Toc159 proteins, Toc159, Toc132, Toc120, and Toc90 have been found in <i><a href="/facts/Arabidopsis_thaliana/wt2IMJsC">Arabidopsis thaliana</a></i>. They vary in the length of their A-domains, which is completely gone in Toc90. Toc132, Toc120, and Toc90 seem to have specialized functions in importing stuff like nonphotosynthetic preproteins, and can't replace Toc159.<a class="footnote-ref" id="fnref:142" href="#fn:142"><sup>142</sup></a> </p> <h4>Toc75</h4> <p>Toc75 is the most abundant protein on the outer chloroplast envelope. It is a <a href="/facts/Transmembrane/0vQH5HrM">transmembrane</a> tube that forms most of the TOC pore itself. Toc75 is a <a href="/facts/%CE%92-barrel/8UMBqHQh">β-barrel</a> channel lined by 16 <a href="/facts/%CE%92-pleated_sheets/B6mwwR6H">β-pleated sheets</a>.<a class="footnote-ref" id="fnref:143" href="#fn:143"><sup>143</sup></a> The hole it forms is about 2.5 <a href="/facts/Nanometers/a98sjHyu">nanometers</a> wide at the ends, and shrinks to about 1.4–1.6 nanometers in diameter at its narrowest point—wide enough to allow partially folded chloroplast preproteins to pass through.<a class="footnote-ref" id="fnref:144" href="#fn:144"><sup>144</sup></a> </p><p>Toc75 can also bind to chloroplast preproteins, but is a lot worse at this than Toc34 or Toc159.<a class="footnote-ref" id="fnref:145" href="#fn:145"><sup>145</sup></a> </p><p><i><a href="/facts/Arabidopsis_thaliana/wt2IMJsC">Arabidopsis thaliana</a></i> has multiple <a href="/facts/Isoforms/oWmzfg4l">isoforms</a> of Toc75 that are named by the <a href="/facts/Chromosomal/FRGf11FC">chromosomal</a> positions of the <a href="/facts/Genes/e1swwPY6">genes</a> that code for them. AtToc75 III is the most abundant of these.<a class="footnote-ref" id="fnref:146" href="#fn:146"><sup>146</sup></a> </p> <h3>The translocon on the inner chloroplast membrane (TIC)</h3> <p>The <a href="/facts/TIC_translocon/WPWPSS6E">TIC translocon</a>, or <i>translocon on the inner chloroplast membrane <a href="/facts/Translocon/qfPhCvM5">translocon</a></i><a class="footnote-ref" id="fnref:147" href="#fn:147"><sup>147</sup></a> is another protein complex that imports proteins across the <a href="/facts/Inner_chloroplast_envelope/JefvL8Dp">inner chloroplast envelope</a>. Chloroplast polypeptide chains probably often travel through the two complexes at the same time, but the TIC complex can also retrieve preproteins lost in the <a href="/facts/Chloroplast_intermembrane_space/lEt0NyqY">intermembrane space</a>.<a class="footnote-ref" id="fnref:148" href="#fn:148"><sup>148</sup></a> </p><p>Like the <a href="/facts/Toc_translocon/WPWPSS6E">TOC translocon</a>, the TIC translocon has a large core <a href="/facts/Protein_complex/GW11Ee34">complex</a> surrounded by some loosely associated peripheral proteins like Tic110, Tic40, and Tic21.<a class="footnote-ref" id="fnref:149" href="#fn:149"><sup>149</sup></a> The core complex weighs about one million <a href="/facts/Dalton_(unit)/IMATU3vf">daltons</a> and contains Tic214, Tic100, Tic56, and Tic20 I, possibly three of each.<a class="footnote-ref" id="fnref:150" href="#fn:150"><sup>150</sup></a> </p> <h4>Tic20</h4> <p>Tic20 is an <a href="/facts/Integral_membrane_protein/Vztpmlu1">integral</a> protein thought to have four <a href="/facts/Transmembrane_domain/D1j0PwSR">transmembrane</a> <a href="/facts/%CE%91-helices/7CESPIYJ">α-helices</a>.<a class="footnote-ref" id="fnref:151" href="#fn:151"><sup>151</sup></a> It is found in the 1 million <a href="/facts/Dalton_(unit)/IMATU3vf">dalton</a> TIC complex.<a class="footnote-ref" id="fnref:152" href="#fn:152"><sup>152</sup></a> Because it is similar to <a href="/facts/Bacterial_protein/Jxmagu3E">bacterial</a> <a href="/facts/Amino_acid/WDxYwBny">amino acid</a> transporters and the <a href="/facts/Mitochondrial/ErHqrdJ1">mitochondrial</a> import protein Tim17<a class="footnote-ref" id="fnref:153" href="#fn:153"><sup>153</sup></a> (<i><a href="/facts/Translocase_of_the_inner_membrane/Ic5vIYvm">translocase</a> on the <a href="/facts/Inner_mitochondrial_membrane/IJIE4o0h">inner mitochondrial membrane</a></i>),<a class="footnote-ref" id="fnref:154" href="#fn:154"><sup>154</sup></a> it has been proposed to be part of the TIC import channel.<a class="footnote-ref" id="fnref:155" href="#fn:155"><sup>155</sup></a> There is no <i><a href="/facts/In_vitro/evp3hAX6">in vitro</a></i> evidence for this though.<a class="footnote-ref" id="fnref:156" href="#fn:156"><sup>156</sup></a> In <i><a href="/facts/Arabidopsis_thaliana/wt2IMJsC">Arabidopsis thaliana</a></i>, it is known that for about every five Toc75 proteins in the outer chloroplast membrane, there are two Tic20 I proteins (the main <a href="/facts/Isoform/oWmzfg4l">form</a> of Tic20 in <a href="/facts/Arabidopsis_thaliana/wt2IMJsC"><i>Arabidopsis</i></a>) in the inner chloroplast membrane.<a class="footnote-ref" id="fnref:157" href="#fn:157"><sup>157</sup></a> </p><p>Unlike Tic214, Tic100, or Tic56, Tic20 has <a href="/facts/Homology_(biology)/muctKlyT">homologous</a> relatives in <a href="/facts/Cyanobacteria/S8bKxIU9">cyanobacteria</a> and nearly all chloroplast lineages, suggesting it evolved before the first chloroplast endosymbiosis. Tic214, Tic100, and Tic56 are unique to <a href="/facts/Chloroplastidan/YAn2Yzck">chloroplastidan</a> chloroplasts, suggesting that they evolved later.<a class="footnote-ref" id="fnref:158" href="#fn:158"><sup>158</sup></a> </p> <h4>Tic214</h4> <p>Tic214 is another TIC core complex protein, named because it weighs just under 214 <a href="/facts/Kilodaltons/IMATU3vf">kilodaltons</a>. It is 1786 <a href="/facts/Amino_acids/WDxYwBny">amino acids</a> long and is thought to have six <a href="/facts/Transmembrane_domains/D1j0PwSR">transmembrane domains</a> on its <a href="/facts/N-terminal/yKYpuaBJ">N-terminal</a> end. Tic214 is notable for being coded for by chloroplast DNA, more specifically the first <a href="/facts/Open_reading_frame/Saams83e">open reading frame</a> <i>ycf1</i>. Tic214 and Tic20 together probably make up the part of the one million <a href="/facts/Dalton_(unit)/IMATU3vf">dalton</a> TIC complex that spans the <a href="/facts/Transmembrane_protein/0vQH5HrM">entire membrane</a>. Tic20 is buried inside the complex while Tic214 is exposed on both sides of the <a href="/facts/Inner_chloroplast_membrane/JefvL8Dp">inner chloroplast membrane</a>.<a class="footnote-ref" id="fnref:159" href="#fn:159"><sup>159</sup></a> </p> <h4>Tic100</h4> <p>Tic100 is a <a href="/facts/Nuclear_genome/5wzCJQlb">nuclear encoded</a> protein that's 871 <a href="/facts/Amino_acids/WDxYwBny">amino acids</a> long. The 871 amino acids collectively weigh slightly less than 100 thousand <a href="/facts/Dalton_(unit)/IMATU3vf">daltons</a>, and since the mature protein probably doesn't lose any amino acids when itself imported into the chloroplast (it has no <a href="/facts/Cleavable_transit_peptide/9oARjq52">cleavable transit peptide</a>), it was named Tic100. Tic100 is found at the edges of the 1 million dalton complex on the side that faces the <a href="/facts/Chloroplast_intermembrane_space/lEt0NyqY">chloroplast intermembrane space</a>.<a class="footnote-ref" id="fnref:160" href="#fn:160"><sup>160</sup></a> </p> <h4>Tic56</h4> <p>Tic56 is also a <a href="/facts/Nuclear_genome/5wzCJQlb">nuclear encoded</a> protein. The <a href="/facts/Preprotein/A1vxb5mN">preprotein</a> its gene encodes is 527 amino acids long, weighing close to 62 thousand <a href="/facts/Dalton_(unit)/IMATU3vf">daltons</a>; the mature form probably undergoes processing that trims it down to something that weighs 56 thousand daltons when it gets imported into the chloroplast. Tic56 is largely embedded inside the 1 million dalton complex.<a class="footnote-ref" id="fnref:161" href="#fn:161"><sup>161</sup></a> </p><p>Tic56 and Tic100 are highly <a href="/facts/Gene_conservation/YAxy2Xa2">conserved</a> among land plants, but they don't resemble any protein whose function is known. Neither has any <a href="/facts/Transmembrane_domains/D1j0PwSR">transmembrane domains</a>.<a class="footnote-ref" id="fnref:162" href="#fn:162"><sup>162</sup></a> </p> <h2 id="see-also">See also</h2> <ul><li><a href="/facts/List_of_sequenced_plastomes/QyAxTbQm">List of sequenced plastomes</a></li> <li><a href="/facts/Mitochondrial_DNA/goC0ex0X">Mitochondrial DNA</a></li></ul> <h2 id="references">References</h2> <ol> <li id="fn:1"><p>Stocking, C. R. & Gifford, E. M. (1959). "Incorporation of thymidine into chloroplasts of Spirogyra". 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