Mycobacterium tuberculosis serine/threonine kinases PknB, PknD, PknE, and PknF phosphorylate multiple FHA domains.
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.
Grundner
Christoph
C
Department of Molecular and Cell Biology, University of California, Berkeley, 94720, USA.
Gay
Laurie M
LM
Alber
Tom
T
D018528:ATP-Binding Cassette Transporters / Q000378:metabolism*; D005982:Glutathione Transferase / Q000378:metabolism; D009169:Mycobacterium tuberculosis / Q000201:enzymology*; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism*; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism*; D017434:Protein Structure, Tertiary
D018528:ATP-Binding Cassette Transporters; C487813:Rv1747 protein, Mycobacterium tuberculosis; D005982:Glutathione Transferase; D011494:Protein Kinases; C475060:PknB protein, Mycobacterium tuberculosis; C112455:PknD protein, Nostoc sp. PCC 7120; C477875:PknE protein, Mycobacterium tuberculosis; C487814:PknF protein, Mycobacterium tuberculosis; D017346:Protein Serine-Threonine Kinases