Molecular Topology of the Transit Peptide during Chloroplast Protein Import
نویسندگان
چکیده
منابع مشابه
Molecular chaperone involvement in chloroplast protein import.
Chloroplasts are organelles of endosymbiotic origin that perform essential functions in plants. They contain about 3000 different proteins, the vast majority of which are nucleus-encoded, synthesized in precursor form in the cytosol, and transported into the chloroplasts post-translationally. These preproteins are generally imported via envelope complexes termed TOC and TIC (Translocon at the O...
متن کاملMolecular chaperones involved in chloroplast protein import.
Transport of cytoplasmically synthesized precursor proteins into chloroplasts, like the protein transport systems of mitochondria and the endoplasmic reticulum, appears to require the action of molecular chaperones. These molecules are likely to be the sites of the ATP hydrolysis required for precursor proteins to bind to and be translocated across the two membranes of the chloroplast envelope....
متن کاملatToc159 is a selective transit peptide receptor for the import of nucleus-encoded chloroplast proteins
The members of the Toc159 family of GTPases act as the primary receptors for the import of nucleus-encoded preproteins into plastids. Toc159, the most abundant member of this family in chloroplasts, is required for chloroplast biogenesis (Bauer, J., K. Chen, A. Hiltbunner, E. Wehrli, M. Eugster, D. Schnell, and F. Kessler. 2000. Nature. 403:203-207) and has been shown to covalently cross-link t...
متن کاملStimulation 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 translocation of precursor proteins. Transit-peptide binding by Tic110 recruits Tic40 binding to Tic110...
متن کاملTransit peptide mutations that impair in vitro and in vivo chloroplast protein import do not affect accumulation of the gamma-subunit of chloroplast ATPase.
We have begun to take a genetic approach to study chloroplast protein import in Chlamydomonas reinhardtii by creating deletions in the transit peptide of the gamma-subunit of chloroplast ATPase-coupling factor 1 (CF1-gamma, encoded by AtpC) and testing their effects in vivo by transforming the altered genes into an atpC mutant, and in vitro by importing mutant precursors into isolated C. reinha...
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ژورنال
عنوان ژورنال: The Plant Cell
سال: 2018
ISSN: 1040-4651,1532-298X
DOI: 10.1105/tpc.18.00172