Post-translational protein import and folding Journal Article


Authors: Höhfeld, J.; Hartl, F. U.
Article Title: Post-translational protein import and folding
Abstract: Significant advances have been made over the past year in analyzing the membrane machineries for the post-translational export of proteins in bacteria and for the import of proteins into mitochondria. Another important development is the identification in mitochondria of homologs of the bacterial heat-shock proteins DnaJ and GrpE, which function together with Hsp70 in membrane translocation and folding of imported proteins. A number of gene products involved in peroxisomal protein uptake have been identified, which are now awaiting biochemical analysis. © 1994.
Keywords: review; nonhuman; protein conformation; protein domain; animal; carboxy terminal sequence; protein protein interaction; protein targeting; gene product; bacteria (microorganisms); bacterial protein; bacterial proteins; protein processing, post-translational; amino terminal sequence; escherichia coli; membrane protein; protein transport; protein folding; mitochondrial membrane; adenosine triphosphatase; mitochondria; membrane transport; mitochondrion; biological transport; cytosol; chaperone; molecular chaperones; membrane receptor; protein precursor; priority journal; chloroplast; proteoliposome; support, non-u.s. gov't; support, u.s. gov't, p.h.s.; peroxisome; thylakoid membrane; chloroplasts
Journal Title: Current Opinion in Cell Biology
Volume: 6
Issue: 4
ISSN: 0955-0674
Publisher: Elsevier Inc.  
Date Published: 1994-08-01
Start Page: 499
End Page: 509
Language: English
DOI: 10.1016/0955-0674(94)90068-x
PROVIDER: scopus
PUBMED: 7986525
DOI/URL:
Notes: Export Date: 14 January 2019 -- Article -- Source: Scopus
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  1. F. Ulrich Hartl
    75 Hartl