Extragenic Suppression analysis of TS mutations using Sec61p
Author(s) -
Sterling Smith
Publication year - 2007
Publication title -
nature precedings
Language(s) - English
Resource type - Journals
ISSN - 1756-0357
DOI - 10.1038/npre.2007.651.1
Subject(s) - endoplasmic reticulum , chaperone (clinical) , membrane protein , protein folding , secretory protein , chemistry , secretory pathway , microbiology and biotechnology , translocon , biophysics , membrane , biochemistry , biology , secretion , medicine , pathology , golgi apparatus
During synthesis, secretory and membrane proteins are cotranslationally translocated into the lumen of the endoplasmic reticulum through an aqueous gated channel. Proper folding, degradation, and transport of many polypeptides depend on a diverse set of helper proteins termed chaperone. I hypothesize that
Sec 61p is a membrane chaperone, which actively directs membrane protein folding.
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