VirA, a coregulator of Ti-specified virulence genes, is phosphorylated in vitro

J Bacteriol. 1990 Feb;172(2):1142-4. doi: 10.1128/jb.172.2.1142-1144.1990.

Abstract

High-level expression of a chimeric virA gene was obtained by replacing the first 524 codons of virA with the first half of trpE. The encoded fusion protein was isolated and found to exhibit autokinase activity. Therefore, a kinase domain is in the C-terminal portion of VirA, and protein phosphorylation may be an important feature of VirA function.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Bacterial Proteins / genetics*
  • Bacterial Proteins / isolation & purification
  • Bacterial Proteins / metabolism
  • Cloning, Molecular
  • Genes, Bacterial*
  • Genes, Regulator*
  • Phosphorylation
  • Protein Kinases / genetics
  • Protein Kinases / metabolism
  • Recombinant Fusion Proteins / isolation & purification
  • Recombinant Fusion Proteins / metabolism
  • Restriction Mapping
  • Rhizobium / genetics*
  • Rhizobium / metabolism
  • Rhizobium / pathogenicity
  • Virulence / genetics
  • Virulence Factors*

Substances

  • Bacterial Proteins
  • Recombinant Fusion Proteins
  • Virulence Factors
  • Protein Kinases