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JXB Advance Access published online on August 8, 2005

Journal of Experimental Botany, doi:10.1093/jxb/eri243
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© The Author [2005]. Published by Oxford University Press [on behalf of the Society for Experimental Biology]. All rights reserved. For Permissions, please e-mail: journals.permissions@oupjournals.org
Received March 14, 2005
Accepted June 7, 2005

REVIEW ARTICLE

Recognition and envelope translocation of chloroplast preproteins

Jocelyn Bédard 1 and Paul Jarvis 1*

1 Department of Biology, University of Leicester, University Road, Leicester LE1 7RH, UK

* To whom correspondence should be addressed.
Paul Jarvis, E-mail: rpj3{at}le.ac.uk


   Abstract

Plastids are a diverse group of plant organelles that perform essential functions including important steps in many biosynthetic pathways. Chloroplasts are the best characterized type of plastid, and constitute the site of oxygenic photosynthesis in plants, a process essential to all higher life forms. It is well established that the majority (>90%) of chloroplast proteins are nucleus-encoded and must be post-translationally imported into these envelope-bound compartments. Most nucleus-encoded chloroplast proteins are translated in precursor form on cytosolic ribosomes, targeted to the chloroplast surface, and then imported across the double-membrane envelope by translocons in the outer and inner envelope membranes of the chloroplast, termed TOC and TIC, respectively. Recently, significant progress has been made in our understanding of how proteins are targeted to the chloroplast surface and translocated across the chloroplast envelope into the stroma. Evidence suggesting the existence of multiple import pathways at the outer envelope membrane for different classes of precursor proteins has been presented. These pathways appear to utilize similar TOC complexes equipped with different combinations of homologous GTPase receptors, providing preprotein recognition specificity.

Keywords: Chloroplast; chloroplast protein import; membrane translocation; organelle biology; plastid; protein targeting; Tic; Toc; translocon.
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