Saccharomyces cerevisiae polo-like kinase, Cdc5 exhibits ATP-dependent Mg²⁺-enhanced kinase activity in vitro.

ABSTRACT: Phosphorylation of proteins on serine/threonine residues represents an important biochemical mechanism to regulate several cellular processes. Polo-like kinases (PLKs) are a family of serine-threonine kinases that play an imminent role in cell cycle regulation in yeast to humans, and thus an important therapeutic target for cancers. The present study provides insights into the enzymatic features of Saccharomyces cerevisiae PLK, Cdc5 using in vitro casein phosphorylation assays. The recombinant yeast PLK, GST-Cdc5 showed maximum casein phosphorylation activity at 30 °C, pH 9 and 45 min of incubation period. GST-Cdc5 exhibited a K_M of 1.35 μM for casein, and high affinity for ATP, since addition of non-radioactive ATP chased out casein phosphorylation by radiolabeled

SUBMITTER: Chauhan S 

PROVIDER: S-EPMC7201137 | biostudies-literature | 2019 Dec

REPOSITORIES: biostudies-literature