Literature DB >> 2494995

Evidence for oligomeric forms of transducins alpha subunit: formation of intermolecular alpha-alpha disulfide linkages.

M Wessling-Resnick1, G L Johnson.   

Abstract

Transducin, the retinal G-protein, is a heterotrimeric protein composed of alpha, beta and gamma subunits. Intermolecular disulfide linkages between the alpha-subunits of transducin molecules are spontaneously formed when the purified G-protein is placed in a non-reducing buffer system. The beta and gamma subunits do not participate in the intermolecular disulfide bridge formation. The alpha-alpha subunit disulfide bonds result in the inhibition of transducin activation by bleached rhodopsin which is restored by reducing the disulfides with dithiothreitol. The trapping of oligomers by disulfide bond formation provides physical evidence for specific intermolecular interactions between alpha-subunits of transducin.

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Year:  1989        PMID： 2494995     DOI： 10.1016/0006-291x(89)90044-2

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN： 0006-291X            Impact factor:   3.575


  4 in total

Review 1.  Oligomerization of G protein-coupled receptors: past, present, and future.

Authors:  Paul S-H Park; Slawomir Filipek; James W Wells; Krzysztof Palczewski
Journal:  Biochemistry       Date:  2004-12-21       Impact factor: 3.162

2.  Mutation of the Gs protein alpha subunit NH2 terminus relieves an attenuator function, resulting in constitutive adenylyl cyclase stimulation.

Authors:  S Osawa; L E Heasley; N Dhanasekaran; S K Gupta; C W Woon; C Berlot; G L Johnson
Journal:  Mol Cell Biol       Date:  1990-06       Impact factor: 4.272

3.  2-Azido-[32P]NAD+, a photoactivatable probe for G-protein structure: evidence for holotransducin oligomers in which the ADP-ribosylated carboxyl terminus of alpha interacts with both alpha and gamma subunits.

Authors:  R R Vaillancourt; N Dhanasekaran; G L Johnson; A E Ruoho
Journal:  Proc Natl Acad Sci U S A       Date:  1990-05       Impact factor: 11.205

4.  The photoactivatable NAD+ analogue [32P]2-azido-NAD+ defines intra- and inter-molecular interactions of the C-terminal domain of the G-protein G alpha t.

Authors:  R R Vaillancourt; N Dhanasekaran; A E Ruoho
Journal:  Biochem J       Date:  1995-11-01       Impact factor: 3.857
  4 in total

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