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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...

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Autores principales: Chou, Ming-Lun, Chu, Chiung-Chih, Chen, Lih-Jen, Akita, Mitsuru, Li, Hsou-min
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 2006
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.
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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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