Multi-functional roles for the polypeptide transport associated domains of Toc75 in chloroplast protein import
Toc75 plays a central role in chloroplast biogenesis in plants as the membrane channel of the protein import translocon at the outer envelope of chloroplasts (TOC). Toc75 is a member of the Omp85 family of bacterial and organellar membrane insertases, characterized by N-terminal POTRA (polypeptide-t...
| Main Authors: | , , , , , , |
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| Format: | Article |
| Language: | English |
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eLife Sciences Publications Ltd
2016-03-01
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| Series: | eLife |
| Subjects: | |
| Online Access: | https://elifesciences.org/articles/12631 |
| _version_ | 1811181398530195456 |
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| author | Yamuna D Paila Lynn GL Richardson Hitoshi Inoue Elizabeth S Parks James McMahon Kentaro Inoue Danny J Schnell |
| author_facet | Yamuna D Paila Lynn GL Richardson Hitoshi Inoue Elizabeth S Parks James McMahon Kentaro Inoue Danny J Schnell |
| author_sort | Yamuna D Paila |
| collection | DOAJ |
| description | Toc75 plays a central role in chloroplast biogenesis in plants as the membrane channel of the protein import translocon at the outer envelope of chloroplasts (TOC). Toc75 is a member of the Omp85 family of bacterial and organellar membrane insertases, characterized by N-terminal POTRA (polypeptide-transport associated) domains and C-terminal membrane-integrated β-barrels. We demonstrate that the Toc75 POTRA domains are essential for protein import and contribute to interactions with TOC receptors, thereby coupling preprotein recognition at the chloroplast surface with membrane translocation. The POTRA domains also interact with preproteins and mediate the recruitment of molecular chaperones in the intermembrane space to facilitate membrane transport. Our studies are consistent with the multi-functional roles of POTRA domains observed in other Omp85 family members and demonstrate that the domains of Toc75 have evolved unique properties specific to the acquisition of protein import during endosymbiotic evolution of the TOC system in plastids. |
| first_indexed | 2024-04-11T09:17:05Z |
| format | Article |
| id | doaj.art-68bb898f2aa24fe9bfa6c750759131a2 |
| institution | Directory Open Access Journal |
| issn | 2050-084X |
| language | English |
| last_indexed | 2024-04-11T09:17:05Z |
| publishDate | 2016-03-01 |
| publisher | eLife Sciences Publications Ltd |
| record_format | Article |
| series | eLife |
| spelling | doaj.art-68bb898f2aa24fe9bfa6c750759131a22022-12-22T04:32:18ZengeLife Sciences Publications LtdeLife2050-084X2016-03-01510.7554/eLife.12631Multi-functional roles for the polypeptide transport associated domains of Toc75 in chloroplast protein importYamuna D Paila0Lynn GL Richardson1Hitoshi Inoue2Elizabeth S Parks3James McMahon4Kentaro Inoue5Danny J Schnell6Department of Plant Biology, Michigan State University, East Lansing, United StatesDepartment of Plant Biology, Michigan State University, East Lansing, United StatesDepartment of Plant Biology, Michigan State University, East Lansing, United StatesDepartment of Plant Biology, Michigan State University, East Lansing, United StatesDepartment of Plant Biology, Michigan State University, East Lansing, United StatesDepartment of Plant Sciences, University of California, Davis, United StatesDepartment of Plant Biology, Michigan State University, East Lansing, United StatesToc75 plays a central role in chloroplast biogenesis in plants as the membrane channel of the protein import translocon at the outer envelope of chloroplasts (TOC). Toc75 is a member of the Omp85 family of bacterial and organellar membrane insertases, characterized by N-terminal POTRA (polypeptide-transport associated) domains and C-terminal membrane-integrated β-barrels. We demonstrate that the Toc75 POTRA domains are essential for protein import and contribute to interactions with TOC receptors, thereby coupling preprotein recognition at the chloroplast surface with membrane translocation. The POTRA domains also interact with preproteins and mediate the recruitment of molecular chaperones in the intermembrane space to facilitate membrane transport. Our studies are consistent with the multi-functional roles of POTRA domains observed in other Omp85 family members and demonstrate that the domains of Toc75 have evolved unique properties specific to the acquisition of protein import during endosymbiotic evolution of the TOC system in plastids.https://elifesciences.org/articles/12631chloroplastprotein importβ-barrelimport channel |
| spellingShingle | Yamuna D Paila Lynn GL Richardson Hitoshi Inoue Elizabeth S Parks James McMahon Kentaro Inoue Danny J Schnell Multi-functional roles for the polypeptide transport associated domains of Toc75 in chloroplast protein import eLife chloroplast protein import β-barrel import channel |
| title | Multi-functional roles for the polypeptide transport associated domains of Toc75 in chloroplast protein import |
| title_full | Multi-functional roles for the polypeptide transport associated domains of Toc75 in chloroplast protein import |
| title_fullStr | Multi-functional roles for the polypeptide transport associated domains of Toc75 in chloroplast protein import |
| title_full_unstemmed | Multi-functional roles for the polypeptide transport associated domains of Toc75 in chloroplast protein import |
| title_short | Multi-functional roles for the polypeptide transport associated domains of Toc75 in chloroplast protein import |
| title_sort | multi functional roles for the polypeptide transport associated domains of toc75 in chloroplast protein import |
| topic | chloroplast protein import β-barrel import channel |
| url | https://elifesciences.org/articles/12631 |
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