tailieunhanh - Báo cáo khoa học: Protein transport into canine pancreatic microsomes A quantitative approach

Transport of presecretory proteins into the mammalian rough endoplasmic reticulum involves a protein translocase that comprises the integral membrane proteins Sec61ap, Sec61bp, and Sec61cp as core components. Electron microscopic analysis of protein translocase in rough micro-somal membranes suggested that between three and four heterotrimeric Sec61p complexes form the central unit of protein translocase. Here we analyzed the stoichiometry of heterotrimericSec61pcomplexespresent incotranslationally active protein translocases of canine pancreatic microsomes and various other lumenal and membrane components believed to be subunits of protein translocase and to be involved in covalentmodifications | Eur. J. Biochem. 271 3200-3207 2004 FEBS 2004 doi Protein transport into canine pancreatic microsomes A quantitative approach Silvia Guth Christian Volzing Anika Muller Martin Jung and Richard Zimmermann Medizinische Biochemie und Molekularbiologie Universitat des Saarlandes Homburg Germany Transport of presecretory proteins into the mammalian rough endoplasmic reticulum involves a protein translocase that comprises the integral membrane proteins Sec61ap Sec61bp and Sec61yp as core components. Electron microscopic analysis of protein translocase in rough microsomal membranes suggested that between three and four heterotrimeric Sec61p complexes form the central unit of protein translocase. Here we analyzed the stoichiometry of heterotrimeric Sec61p complexes present in cotranslationally active protein translocases of canine pancreatic microsomes and various other lumenal and membrane components believed to be subunits of protein translocase and to be involved in covalent modifications. Based on these numbers the capacity for cotranslational transport was estimated for the endoplasmic reticulum of the human pancreas. Keywords endoplasmic reticulum mammalian microsomes protein secretion protein transport pancreas. Transport of presecretory proteins into mammalian rough microsomes involves cleavable signal peptides at the N-terminus of the precursor proteins and a protein translocase in the microsomal membrane 1 . Typically transport occurs as a sequence of three consecutive steps namely a specific membrane association of the precursor protein also termed targeting b membrane insertion and c completion of translocation. Specific membrane association of precursors in cotranslational transport involves two ribonu-cleoparticles - the ribosome 2 and the signal recognition particle SRP 3 - as well as their receptors on the endoplasmic reticulum ER surface the SRP and ribosome receptors 4 5 . Protein translocase a mediates both membrane .

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