Mycobacterium tuberculosis serine/threonine kinases PknB, PknD, PknE, and PknF phosphorylate multiple FHA domains

Protein Sci. 2005 Jul;14(7):1918-21. doi: 10.1110/ps.051413405.

Abstract

The physiologic roles and the substrates of the Mycobacterium tuberculosis (Mtb) serine/threonine kinases are largely unknown. Here, we report six novel interactions of PknB, PknD, PknE, and PknF with the Forkhead-Associated (FHA) domains of Rv0020c and the putative ABC transporter Rv1747. Purified PknB and PknF kinase domains phosphorylated multiple FHA-domain proteins in vitro. Although they remain to be verified in vivo, these reactions suggest a web of interactions between STPKs and FHA domains.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • ATP-Binding Cassette Transporters / metabolism*
  • Glutathione Transferase / metabolism
  • Mycobacterium tuberculosis / enzymology*
  • Phosphorylation
  • Protein Kinases / metabolism*
  • Protein Structure, Tertiary
  • Protein-Serine-Threonine Kinases / metabolism*

Substances

  • ATP-Binding Cassette Transporters
  • Rv1747 protein, Mycobacterium tuberculosis
  • Glutathione Transferase
  • Protein Kinases
  • PknB protein, Mycobacterium tuberculosis
  • PknD protein, Nostoc sp. PCC 7120
  • PknE protein, Mycobacterium tuberculosis
  • PknF protein, Mycobacterium tuberculosis
  • Protein-Serine-Threonine Kinases