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Repetitive Segmental Structure of the Transducin β Subunit: Homology with the CDC4 Gene and Identification of Related mRNAs

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TLDR
The results suggest that the mRNAs in retina are the processed products of a small number of closely related genes or of a single highly complex beta gene.
Abstract
Retinal transducin, a guanine nucleotide regulatory protein (referred to as a G protein) that activates a cGMP phosphodiesterase in photoreceptor cells, is comprised of three subunits. We have identified and analyzed cDNA clones of the bovine transducin beta subunit that may be highly conserved or identical to that in other G proteins. From the cDNA nucleotide sequence of the entire coding region, the primary structure of a 340-amino acid protein was deduced. The encoded beta subunit has a Mr of 37,375 and is comprised of repetitive homologous segments arranged in tandem. Furthermore, significant homology in primary structure and segmental sequence exists between the beta subunit and the yeast CDC4 gene product. The Mr 37,375 beta subunit polypeptide is encoded by a 2.9-kilobase (kb) mRNA. However, there exists in retina other beta-related mRNAs that are divergent from the 2.9-kb mRNA on the basis of oligonucleotide and primer-extended probe hybridizations. All mammalian tissues and clonal cell lines that have been examined contain at least two beta-related mRNAs, usually 1.8 and 2.9 kb in length. These results suggest that the mRNAs are the processed products of a small number of closely related genes or of a single highly complex beta gene.

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Diversity of G proteins in signal transduction.

TL;DR: The heterotrimeric guanine nucleotide-binding proteins acting as switches that regulate information processing circuits connecting cell surface receptors to a variety of effectors generate the pathways that modulate cellular responses to complex chemical signals.
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The ancient regulatory-protein family of WD-repeat proteins

TL;DR: WD proteins are made up of highly conserved repeating units usually ending with Trp-Asp (WD), and criteria for grouping such proteins into functional subfamilies are defined.
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G PROTEIN MECHANISMS: Insights from Structural Analysis

TL;DR: This review is concerned with the structures and mechanisms of a superfamily of regulatory GTP hydrolases (G proteins), which include Ras and its close homologs, translation elongation factors, and heterotrimeric G proteins.
Journal ArticleDOI

The structure of the G protein heterotrimer Giα1β1γ2

TL;DR: The structure of the G protein heterotrimer Gi alpha 1(GDP)beta 1 gamma 2 (at 2.3 A) reveals two nonoverlapping regions of contact between alpha and beta, an extended interface between beta and nearly all of gamma, and limited interaction of alpha with gamma as mentioned in this paper.
Journal ArticleDOI

Roles of G protein subunits in transmembrane signalling.

TL;DR: A family of proteins called G proteins couples cell surface receptors to a variety of enzymes and ion channels, and an important question is how signals remain specific as they cross the cell membrane.
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