NDLI: Molecular cloning of beta 3 subunit, a third form of the G protein beta-subunit polypeptide.

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Molecular cloning of beta 3 subunit, a third form of the G protein beta-subunit polypeptide.

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Molecular cloning of beta 3 subunit, a third form of the G protein beta-subunit polypeptide.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Smallwood, P. M. Levine, M. A. Moen, P. T. Helman, L. J. Ahn, T. G.
Description	Author Affiliation: Levine MA ( Department of Medicine, Johns Hopkins University School of Medicine, Baltimore, MD 21205.);
Abstract	The signal-transducing guanine nucleotide-binding regulatory (G) proteins are heterotrimers composed of three subunits--alpha, beta, and gamma. Although multiple distinctive forms of the alpha subunit have been described, only two forms of the beta subunits of the G proteins have been identified. To investigate further the structural diversity of the beta subunits, we screened bovine and human retina cDNA libraries and isolated clones encoding three distinct types of G protein beta subunit. One form was identical to previously isolated beta 1-subunit cDNA clones that encode the 36-kDa form of the beta subunit, whereas a second form was identical to previously described beta 2 cDNAs that encode the 35-kDa beta isoform. In addition, we identified another species, designated beta 3 subunit, which encodes a third distinct form of the beta subunit. The beta 3-subunit cDNA corresponds to a 2.0-kilobase mRNA expressed in all tissues and clonal cell lines examined. Nucleotide sequence analysis indicates that the encoded peptide consists of 340-amino acid residues with a Mr of 37,221. The amino acid sequences of the three beta subunits are closely related: 83% identity between beta 1 and beta 3 subunits and 81% identity between beta 2 and beta 3 subunits. By contrast, the 3'-untranslated regions of the three cDNAs show no significant homology. Our data support the hypothesis that a family of beta-subunit polypeptides exists and extend understanding of beta-subunit structure.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	6
Volume Number	87
Language	English
Publisher	National Academy of Sciences
Publisher Date	1990-04-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Cloning, Molecular GTP-Binding Proteins Genetics Amino Acid Sequence Animals DNA Gene Library Macromolecular Substances Molecular Sequence Data Nucleic Acid Hybridization Oligonucleotide Probes RNA, Messenger Retina Metabolism Sequence Homology, Nucleic Acid Comparative Study Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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