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• W2002863315 abstract "Protein translocation into the endoplasmic reticulum occurs at pore-forming structures known as translocons. In yeast, two different targeting pathways converge at a translocation pore formed by the Sec61 complex. The signal recognition particle-dependent pathway targets nascent precursors co-translationally, whereas the Sec62p-dependent pathway targets polypeptides post-translationally. In addition to the Sec61 complex, both pathways also require Sec63p, an integral membrane protein of the Hsp40 family, and Kar2p, a soluble Hsp70 located in the ER lumen. Using a series of mutant alleles, we demonstrate that a conserved Brl (Brr2-like) domain in the COOH-terminal cytosolic region of Sec63p is essential for function both <i>in vivo</i> and <i>in vitro</i>. We further demonstrate that this domain is required for assembly of two oligomeric complexes of 350 and 380 kDa, respectively. The larger of these corresponds to the heptameric SEC complex required for post-translational translocation. However, the 350-kDa complex represents a newly defined hexameric SEC′ complex comprising Sec61p, Sss1p, Sbh1p, Sec63p, Sec71p, and Sec72p. Our data indicate that the SEC′ complex is required for co-translational protein translocation across the yeast ER membrane." @default.
• W2002863315 created "2016-06-24" @default.
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• W2002863315 date "2006-03-01" @default.
• W2002863315 modified "2023-10-16" @default.
• W2002863315 title "The Brl Domain in Sec63p Is Required for Assembly of Functional Endoplasmic Reticulum Translocons" @default.
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• W2002863315 doi "https://doi.org/10.1074/jbc.m511402200" @default.
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