JXB Advance Access originally published online on August 8, 2005
Journal of Experimental Botany 2005 56(419):2287-2320; doi:10.1093/jxb/eri243
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REVIEW ARTICLE |
Recognition and envelope translocation of chloroplast preproteins
Department of Biology, University of Leicester, University Road, Leicester LE1 7RH, UK
* To whom correspondence should be addressed. Fax: +44 (0)116 252 3330. E-mail: rpj3{at}le.ac.uk
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.
Key words: Chloroplast, chloroplast protein import, membrane translocation, organelle biology, plastid, protein targeting, Tic, Toc, translocon
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