A novel tyrosine-phosphorylated protein inhibiting the growth of Streptomyces cells

Biochem Biophys Res Commun. 2009 Aug 7;385(4):534-8. doi: 10.1016/j.bbrc.2009.05.091. Epub 2009 May 24.

Abstract

Very few of the tyrosine-phosphorylated proteins in Streptomyces have been identified. Here, we identify a tyrosine-phosphorylated protein from Streptomyces coelicolor A3(2), designated as SCO5717. The protein possesses Walker motifs and a tyrosine cluster at the C-terminus. When sco5717 harboring its own promoter was introduced into the S. coelicolor cell, the growth was inhibited. An sco5717-disrupted mutant formed aerial mycelium earlier than the wild-type strain, suggesting that SCO5717 controls the cell growth of S. coelicolor. Although the recombinant SCO5717 showed an ATPase activity, it lacked self-phosphorylation ability, suggesting that SCO5717 is a novel tyrosine-phosphorylated protein, which is distinguishable from bacterial protein tyrosine kinases known so far.

MeSH terms

  • Amino Acid Motifs
  • Amino Acid Sequence
  • Molecular Sequence Data
  • Phosphorylation
  • Protein-Tyrosine Kinases / chemistry
  • Protein-Tyrosine Kinases / genetics
  • Protein-Tyrosine Kinases / metabolism*
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism
  • Streptomyces coelicolor / enzymology*
  • Streptomyces coelicolor / genetics
  • Streptomyces coelicolor / growth & development*
  • Tyrosine / metabolism*

Substances

  • Recombinant Proteins
  • Tyrosine
  • Protein-Tyrosine Kinases