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Stimulation of transit-peptide release and ATP hydrolysis by a cochaperone during protein import into chloroplasts
Three components of the chloroplast protein translocon, Tic110, Hsp93 (ClpC), and Tic40, have been shown to be important for protein translocation across the inner envelope membrane into the stroma. We show the molecular interactions among these three components that facilitate processing and transl...
Autores principales: | , , , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
2006
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2064699/ https://www.ncbi.nlm.nih.gov/pubmed/17158958 http://dx.doi.org/10.1083/jcb.200609172 |
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author | Chou, Ming-Lun Chu, Chiung-Chih Chen, Lih-Jen Akita, Mitsuru Li, Hsou-min |
author_facet | Chou, Ming-Lun Chu, Chiung-Chih Chen, Lih-Jen Akita, Mitsuru Li, Hsou-min |
author_sort | Chou, Ming-Lun |
collection | PubMed |
description | Three components of the chloroplast protein translocon, Tic110, Hsp93 (ClpC), and Tic40, have been shown to be important for protein translocation across the inner envelope membrane into the stroma. We show the molecular interactions among these three components that facilitate processing and translocation of precursor proteins. Transit-peptide binding by Tic110 recruits Tic40 binding to Tic110, which in turn causes the release of transit peptides from Tic110, freeing the transit peptides for processing. The Tic40 C-terminal domain, which is homologous to the C terminus of cochaperones Sti1p/Hop and Hip but with no known function, stimulates adenosine triphosphate hydrolysis by Hsp93. Hsp93 dissociates from Tic40 in the presence of adenosine diphosphate, suggesting that Tic40 functions as an adenosine triphosphatase activation protein for Hsp93. Our data suggest that chloroplasts have evolved the Tic40 cochaperone to increase the efficiency of precursor processing and translocation. |
format | Text |
id | pubmed-2064699 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2006 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-20646992007-11-29 Stimulation of transit-peptide release and ATP hydrolysis by a cochaperone during protein import into chloroplasts Chou, Ming-Lun Chu, Chiung-Chih Chen, Lih-Jen Akita, Mitsuru Li, Hsou-min J Cell Biol Research Articles Three components of the chloroplast protein translocon, Tic110, Hsp93 (ClpC), and Tic40, have been shown to be important for protein translocation across the inner envelope membrane into the stroma. We show the molecular interactions among these three components that facilitate processing and translocation of precursor proteins. Transit-peptide binding by Tic110 recruits Tic40 binding to Tic110, which in turn causes the release of transit peptides from Tic110, freeing the transit peptides for processing. The Tic40 C-terminal domain, which is homologous to the C terminus of cochaperones Sti1p/Hop and Hip but with no known function, stimulates adenosine triphosphate hydrolysis by Hsp93. Hsp93 dissociates from Tic40 in the presence of adenosine diphosphate, suggesting that Tic40 functions as an adenosine triphosphatase activation protein for Hsp93. Our data suggest that chloroplasts have evolved the Tic40 cochaperone to increase the efficiency of precursor processing and translocation. The Rockefeller University Press 2006-12-18 /pmc/articles/PMC2064699/ /pubmed/17158958 http://dx.doi.org/10.1083/jcb.200609172 Text en Copyright © 2006, The Rockefeller University Press This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/). |
spellingShingle | Research Articles Chou, Ming-Lun Chu, Chiung-Chih Chen, Lih-Jen Akita, Mitsuru Li, Hsou-min Stimulation of transit-peptide release and ATP hydrolysis by a cochaperone during protein import into chloroplasts |
title | Stimulation of transit-peptide release and ATP hydrolysis by a cochaperone during protein import into chloroplasts |
title_full | Stimulation of transit-peptide release and ATP hydrolysis by a cochaperone during protein import into chloroplasts |
title_fullStr | Stimulation of transit-peptide release and ATP hydrolysis by a cochaperone during protein import into chloroplasts |
title_full_unstemmed | Stimulation of transit-peptide release and ATP hydrolysis by a cochaperone during protein import into chloroplasts |
title_short | Stimulation of transit-peptide release and ATP hydrolysis by a cochaperone during protein import into chloroplasts |
title_sort | stimulation of transit-peptide release and atp hydrolysis by a cochaperone during protein import into chloroplasts |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2064699/ https://www.ncbi.nlm.nih.gov/pubmed/17158958 http://dx.doi.org/10.1083/jcb.200609172 |
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