Brazill D T, Thorner J, Martin G S
Department of Molecular and Cell Biology, University of California at Berkeley, 94720, USA.
J Bacteriol. 1997 Jul;179(13):4415-8. doi: 10.1128/jb.179.13.4415-4418.1997.
An interaction between the Saccharomyces cerevisiae protein kinase Mck1 and pyruvate kinase (Pyk1) was detected by using the two-hybrid method. Purified Mck1 was able to phosphorylate purified Pyk1 on Ser in vitro. Pyruvate kinase activity was elevated in mck1 delta cells. Several of the phenotypes of mck1 delta mutants are similar to those observed in cells overexpressing PYK1. Co-overexpression of MCK1 suppressed all of the phenotypes associated with PYK1 overexpression. These results indicate that Mck1 negatively regulates pyruvate kinase activity, possibly by direct phosphorylation.
利用双杂交方法检测到酿酒酵母蛋白激酶Mck1与丙酮酸激酶(Pyk1)之间存在相互作用。纯化的Mck1能够在体外将纯化的Pyk1的丝氨酸残基磷酸化。在mck1Δ细胞中丙酮酸激酶活性升高。mck1Δ突变体的几种表型与在过表达PYK1的细胞中观察到的表型相似。MCK1的共过表达抑制了与PYK1过表达相关的所有表型。这些结果表明,Mck1可能通过直接磷酸化对丙酮酸激酶活性进行负调控。