Cloning and characterization of the pknA gene from Streptomyces coelicolor A3(2), coding for the Mn2+ dependent protein Ser/Thr kinase

Biochem Biophys Res Commun. 2000 Dec 29;279(3):942-8. doi: 10.1006/bbrc.2000.4054.

Abstract

A gene pknA, coding for an eukaryotic-type protein Ser/Thr kinase, was cloned from the Streptomyces coelicolor A3(2) chromosome. The PknA protein kinase, containing the C-terminal eukaryotic-type kinase domain with an N-terminal extension, was expressed in Escherichia coli and Streptomyces lividans. The affinity purified MBP-PknA fusion protein was assayed for kinase activity that showed its ability to autophosphorylate in vitro in the presence of [gamma-32P]ATP. The activity was Mn2+ dependent. The preautophosphorylated kinase phosphorylated at least two proteins (sizes 30 and 32 kDa) in the S. coelicolor J1501 cell-free extracts of all developmental stages. The larger of them was also phosphorylated in vitro by an endogenous protein kinase in late stages extracts, but not earlier. Although Mn2+ dependent protein phosphorylation has previously been described in Streptomyces, this is the first report of a gene encoding such an enzyme in this genus.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins*
  • Base Sequence
  • Cloning, Molecular
  • DNA, Bacterial / analysis
  • Escherichia coli
  • Manganese / metabolism
  • Molecular Sequence Data
  • Phenotype
  • Phosphorylation
  • Protein Kinases / genetics*
  • Protein Kinases / isolation & purification
  • Protein Kinases / metabolism
  • Protein Serine-Threonine Kinases / genetics
  • Protein Serine-Threonine Kinases / metabolism
  • Sequence Analysis, DNA
  • Streptomyces / enzymology
  • Streptomyces / genetics*

Substances

  • Bacterial Proteins
  • DNA, Bacterial
  • Manganese
  • Protein Kinases
  • PknA protein, Nostoc sp. PCC 7120
  • Protein Serine-Threonine Kinases