Protein ubiquitination is regulated by phosphorylation. An in vitro study.
作者： S.K. Kong , P.B. Chock
DOI: 10.1016/S0021-9258(19)49696-8
关键词:
摘要: Protein ubiquitination has been implicated in ATP-dependent protein turnover and a number of biological processes eukaryotic cells. The activating enzyme, E1, ubiquitin carrier protein, E2, are two essential enzymes the machinery. Using purified E1 E2 from rabbit reticulocytes various kinases, which include cAMP-dependent kinase, kinase C, tyrosine we demonstrated that is phosphorylated by with stoichiometry 0.65 mol phosphate/mol one isoforms, E2(32kDa), to 2 eq protein. Phosphorylation causes 2-fold enhancement its activity as monitored ubiquitin-dependent ATP equilibrium PPi exchange. When 1 phosphate was incorporated into 2.4-fold activation also observed for catalyze histone H2A. regulatory significance this finding discussed.
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