NDLI: Homologs of the yeast Sec complex subunits Sec62p and Sec63p are abundant proteins in dog pancreas microsomes.

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Homologs of the yeast Sec complex subunits Sec62p and Sec63p are abundant proteins in dog pancreas microsomes.

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Homologs of the yeast Sec complex subunits Sec62p and Sec63p are abundant proteins in dog pancreas microsomes.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Haas, I. G. Zimmermann, R. Lerner, M. Dudek, J. Skowronek, M. H. Bies, C. Nastainczyk, W. Tyedmers, J. Heim, N. Volkmer, J.
Description	Author Affiliation: Tyedmers J ( Medizinische Biochemie und Molekularbiologie, Universität des Saarlandes, D-66421 Homburg, Germany.);
Abstract	Cotranslational protein transport into dog pancreas microsomes involves the Sec61p complex plus a luminal heat shock protein 70. Posttranslational protein transport into the yeast endoplasmic reticulum (ER) involves the so-called Sec complex in the membrane, comprising a similar Sec61p subcomplex, the putative signal peptide receptor subcomplex, and the heat shock protein 40-type subunit, Sec63p, plus a luminal heat shock protein 70. Recently, human homologs of yeast proteins Sec62p and Sec63p were discovered. Here we determined the concentrations of these two membrane proteins in dog pancreas microsomes and observed that the canine homologs of yeast proteins Sec62p and Sec63p are abundant proteins, present in almost equimolar concentrations as compared with Sec61alphap monomers. Furthermore, we detected fractions of these two proteins in association with each other as well as with the Sec61p complex. The J domain of the human Sec63p was shown to interact with immunoglobulin heavy chain binding protein. Thus, the membrane of the mammalian ER contains components, known from the posttranslationally operating protein translocase in yeast. We suggest that these components are required for efficient cotranslational protein transport into the mammalian ER as well as for other transport processes.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	13
Volume Number	97
Language	English
Publisher	National Academy of Sciences
Publisher Date	2000-07-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Fungal Proteins Genetics Metabolism Heat-Shock Proteins Membrane Proteins Membrane Transport Proteins Microsomes Pancreas Saccharomyces Cerevisiae Proteins Amino Acid Sequence Animals Molecular Sequence Data Ultrastructure Saccharomyces Cerevisiae Sequence Homology, Amino Acid Research Support, Non-U.S. Gov't Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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