doi: 10.1126/science.277.5328.938.
Protein transport by purified yeast Sec complex and Kar2p without membranes
Affiliations
- PMID: 9252322
- DOI: 10.1126/science.277.5328.938
Item in Clipboard
Protein transport by purified yeast Sec complex and Kar2p without membranes
Science.
.
Erratum in
- Science 1997 Sep 19;277(5333):1749
Abstract
Posttranslational protein translocation across the endoplasmic reticulum membrane of yeast requires a seven-component transmembrane complex (the Sec complex) in collaboration with the lumenal Kar2 protein (Kar2p). A translocation substrate was initially bound to the cytosolic face of the purified Sec complex in a signal-sequence-dependent but Kar2p- and nucleotide-independent manner. In a subsequent reaction, in which Kar2p interacted with the lumenal face of the Sec complex and hydrolyzed adenosine triphosphate, the substrate moved through a channel formed by the Sec complex and was released at the lumenal end. Movement through the channel occurred in detergent solution in the absence of a lipid bilayer.
Similar articles
-
Posttranslational protein transport in yeast reconstituted with a purified complex of Sec proteins and Kar2p.Cell. 1995 May 19;81(4):561-70. doi: 10.1016/0092-8674(95)90077-2. Cell. 1995. PMID: 7758110
-
Signal sequence recognition in posttranslational protein transport across the yeast ER membrane.Cell. 1998 Sep 18;94(6):795-807. doi: 10.1016/s0092-8674(00)81738-9. Cell. 1998. PMID: 9753326
-
Interaction between BiP and Sec63p is required for the completion of protein translocation into the ER of Saccharomyces cerevisiae.J Cell Biol. 1995 Dec;131(5):1163-71. doi: 10.1083/jcb.131.5.1163. J Cell Biol. 1995. PMID: 8522580 Free PMC article.
-
The role of molecular chaperones in protein transport into the mammalian endoplasmic reticulum.Biol Chem. 1998 Mar;379(3):275-82. Biol Chem. 1998. PMID: 9563822 Review.
-
Protein targeting to the endoplasmic reticulum in yeast. 1997 Fleming Lecture.Microbiology (Reading). 1999 May;145 ( Pt 5):991-998. doi: 10.1099/13500872-145-5-991. Microbiology (Reading). 1999. PMID: 10376813 Review. No abstract available.
Cited by
-
Recognition of a subset of signal sequences by Ssh1p, a Sec61p-related protein in the membrane of endoplasmic reticulum of yeast Saccharomyces cerevisiae.Mol Biol Cell. 2002 Jul;13(7):2223-32. doi: 10.1091/mbc.01-10-0518. Mol Biol Cell. 2002. PMID: 12134063 Free PMC article.
-
Structure of the posttranslational Sec protein-translocation channel complex from yeast.Science. 2019 Jan 4;363(6422):84-87. doi: 10.1126/science.aav6740. Epub 2018 Dec 13. Science. 2019. PMID: 30545845 Free PMC article.
-
Sec63p and Kar2p are required for the translocation of SRP-dependent precursors into the yeast endoplasmic reticulum in vivo.EMBO J. 2001 Jan 15;20(1-2):262-71. doi: 10.1093/emboj/20.1.262. EMBO J. 2001. PMID: 11226176 Free PMC article.
-
Chaperone-mediated reflux of secretory proteins to the cytosol during endoplasmic reticulum stress.Proc Natl Acad Sci U S A. 2019 Jun 4;116(23):11291-11298. doi: 10.1073/pnas.1904516116. Epub 2019 May 17. Proc Natl Acad Sci U S A. 2019. PMID: 31101715 Free PMC article.
-
Emerging View on the Molecular Functions of Sec62 and Sec63 in Protein Translocation.Int J Mol Sci. 2021 Nov 25;22(23):12757. doi: 10.3390/ijms222312757. Int J Mol Sci. 2021. PMID: 34884562 Free PMC article. Review.
Publication types
MeSH terms
Substances
Grants and funding
LinkOut - more resources
Full Text Sources
Molecular Biology Databases
