The phosphorylation state of transducin beta-subunits

Autor: T. G. Orlova, N. Ya. Orlov, A. R. Nezvetsky, D. N. Orlov, O. V. Petrukhin
Rok vydání: 2014
Předmět:
Zdroj: Scopus-Elsevier
ISSN: 1555-6654
0006-3509
DOI: 10.1134/s0006350914050194
Popis: The supposition that nucleoside diphosphate kinase is the enzyme that phosphorylates transducin beta-subunits at one of the histidine residues (His 266) has been analyzed. It is based on the reasons that (1) this enzyme is multifunctional and plays in particular the role of protein histidine kinase; and (2) the phosphorylated beta-subunit of transducin may activate transducin via the mechanism of transphosphorylation. Nevertheless, in our experiments, in which different forms of transducin preparations were incubated with α- and β-isoforms of recombinant rat NDP kinase in the presence of [γ32P]ATP or [γ32P]GTP (specific activity of about 1 Ci/mmol) followed by separation of proteins by electrophoresis and gel radio-autography, we have not succeeded in observing phosphorylation of the transducin beta-subunit. The negative result of our experiments most likely implies that the major part of transducin beta-subunits in the preparations has already been phosphorylated via a process that takes place in vivo.
Databáze: OpenAIRE
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