NDLI: Assembly of a heterooligomeric asialoglycoprotein receptor complex during cell-free translation.

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Assembly of a heterooligomeric asialoglycoprotein receptor complex during cell-free translation.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Doyle, D. Sawyer, J. T.
Description	Author Affiliation: Sawyer JT ( Department of Biological Sciences, State University of New York, Buffalo 14260.);
Abstract	We have translated RNAs for the two rat asialoglycoprotein receptor polypeptides together in a cell-free system containing dog pancreatic microsomes and immunoprecipitated the products with antibodies that distinguish the two proteins. In this system the proteins oligomerize, as judged by their coprecipitation with either of the subunit-specific antisera. Oligomerization does not occur between subunits synthesized without microsomes or between subunits synthesized on separate microsomes mixed during detergent solubilization. Thus, oligomerization occurs within the microsomal membrane. We calculate that oligomerization proceeds with an efficiency of approximately 85%. The receptor complex appears to represent a specific oligomer because it excludes a third membrane glycoprotein synthesized in the same reaction. Oligomerization of the asialoglycoprotein receptor in vitro should provide a useful system to study the assembly of a membrane-protein complex.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	12
Volume Number	87
Language	English
Publisher	National Academy of Sciences
Publisher Date	1990-07-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Protein Biosynthesis Receptors, Immunologic Genetics Animals Asialoglycoprotein Receptor Cell-Free System Macromolecular Substances Microsomes Metabolism Pancreas Plasmids RNA Transcription, Genetic Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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