New Insights into the Mechanism of Chloroplast Protein Import and Its Integration with Protein Quality Control, Organelle Biogenesis and Development
Journal of Molecular Biology, ISSN: 0022-2836, Vol: 427, Issue: 5, Page: 1038-1060
2015
- 119Citations
- 180Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
- Citations119
- Citation Indexes119
- 119
- CrossRef89
- Captures180
- Readers180
- 180
Review Description
The translocons at the outer (TOC) and the inner (TIC) envelope membranes of chloroplasts mediate the targeting and import of several thousand nucleus-encoded preproteins that are required for organelle biogenesis and homeostasis. The cytosolic events in preprotein targeting remain largely unknown, although cytoplasmic chaperones have been proposed to facilitate delivery to the TOC complex. Preprotein recognition is mediated by the TOC GTPase receptors Toc159 and Toc34. The receptors constitute a GTP-regulated switch, which initiates membrane translocation via Toc75, a member of the Omp85 ( o uter m embrane p rotein 85 )/TpsB ( t wo- p artner s ecretion system B ) family of bacterial, plastid and mitochondrial β-barrel outer membrane proteins. The TOC receptor systems have diversified to recognize distinct sets of preproteins, thereby maximizing the efficiency of targeting in response to changes in gene expression during developmental and physiological events that impact organelle function. The TOC complex interacts with the TIC translocon to allow simultaneous translocation of preproteins across the envelope. Both the two inner membrane complexes, the Tic110 and 1 MDa complexes, have been implicated as constituents of the TIC translocon, and it remains to be determined how they interact to form the TIC channel and assemble the import-associated chaperone network in the stroma that drives import across the envelope membranes. This review will focus on recent developments in our understanding of the mechanisms and diversity of the TOC–TIC systems. Our goal is to incorporate these recent studies with previous work and present updated or revised models for the function of TOC–TIC in protein import.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0022283614004598; http://dx.doi.org/10.1016/j.jmb.2014.08.016; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=84923074903&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/25174336; https://linkinghub.elsevier.com/retrieve/pii/S0022283614004598
Elsevier BV
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