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Plastid Protein Targeting: Preprotein Recognition and Translocation.

Authors
  • Chotewutmontri, P1
  • Holbrook, K2
  • Bruce, B D3
  • 1 Graduate School of Genome Science and Technology, University of Tennessee, Knoxville, TN, United States.
  • 2 University of Tennessee, Knoxville, TN, United States.
  • 3 Graduate School of Genome Science and Technology, University of Tennessee, Knoxville, TN, United States; University of Tennessee, Knoxville, TN, United States. Electronic address: [email protected]
Type
Published Article
Journal
International review of cell and molecular biology
Publication Date
2017
Volume
330
Pages
227–294
Identifiers
DOI: 10.1016/bs.ircmb.2016.09.006
PMID: 28215533
Source
Medline
Keywords
License
Unknown

Abstract

Eukaryotic organisms are defined by their endomembrane system and various organelles. The membranes that define these organelles require complex protein sorting and molecular machines that selectively mediate the import of proteins from the cytosol to their functional location inside the organelle. The plastid possibly represents the most complex system of protein sorting, requiring many different translocons located in the three membranes found in this organelle. Despite having a small genome of its own, the vast majority of plastid-localized proteins is nuclear encoded and must be posttranslationally imported from the cytosol. These proteins are encoded as a larger molecular weight precursor that contains a special "zip code," a targeting sequence specific to the intended final destination of a given protein. The "zip code" is located at the precursor N-terminus, appropriately called a transit peptide (TP). We aim to provide an overview of plastid trafficking with a focus on the mechanism and regulation of the general import pathway, which serves as a central import hub for thousands of proteins that function in the plastid. We extend comparative analysis of plant proteomes to develop a better understanding of the evolution of TPs and differential TP recognition. We also review alternate import pathways, including vesicle-mediated trafficking, dual targeting, and import of signal-anchored and tail-anchored proteins.

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