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

Christoph Grundner; Laurie M Gay; Tom Alber

doi:10.1110/ps.051413405

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.

Authors

Christoph Grundner¹, Laurie M Gay, Tom Alber

Affiliation

¹ Department of Molecular and Cell Biology, University of California, Berkeley, 94720, USA.

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 Serine-Threonine Kinases / metabolism*
Protein Structure, Tertiary

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