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FOR THE RECORD

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

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

(RECEIVED February 15, 2005; FINAL REVISION April 20, 2005; ACCEPTED April 21, 2005)

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.

Keywords: FHA domain; protein phosphorylation; serine/threonine protein kinase; signaling

Article and publication are at http://www.proteinscience.org/cgi/doi/10.1110/ps.051413405.

Reprint requests to: Tom Alber, Department of Molecular and Cell Biology, 339 Hildebrand Hall, University of California, Berkeley, CA 94720, USA; e-mail: tom{at}ucxray.berkeley.edu; fax: (510) 643-9290.

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