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J. Biol. Chem., Vol. 281, Issue 52, 40107-40113, December 29, 2006

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GTPase Activity of Mycobacterial FtsZ Is Impaired Due to Its Transphosphorylation by the Eukaryotic-type Ser/Thr Kinase, PknA^*

From the Institute of Microbial Technology, Sector 39A, Chandigarh 160 036, India

FtsZ, a homolog of eukaryotic tubulin, is involved in the process of cell division, particularly in septum formation in bacteria. The primary amino acid sequences of this protein are fairly conserved in prokaryotes. We observed that a eukaryotic-type Ser/Thr protein kinase, PknA from Mycobacterium tuberculosis, when expressed in Escherichia coli exhibited cell elongation due to a defect in septum formation. We found that FtsZ either from Escherichia coli (eFtsZ) or from M. tuberculosis (mFtsZ) was phosphorylated on co-expression with PknA. Consistent with these observations, solid phase binding and in vitro kinase assays revealed the ability of PknA to interact with mFtsZ protein and also to phosphorylate it. We, therefore, ascertained mFtsZ as a substrate of PknA. Furthermore, the phosphorylated mFtsZ exhibited impairment in its GTP hydrolysis and polymerization abilities. Thus, our results highlighted the ability of PknA to phosphorylate as well as to regulate the functionality of FtsZ, the protein central to cell division throughout the bacterial lineage.

Received for publication, July 31, 2006 , and in revised form, October 11, 2006.

^* This work was supported in part by grants from the Indian Council of Medical Research, New Delhi, India and by Network Project Grant SMM 003 from the Council of Scientific and Industrial Research. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ Recipient of Senior Research Fellowship from the Council of Scientific and Industrial Research, New Delhi, India.

² To whom correspondence should be addressed. Tel.: 91-172-2690751; Fax: 91-172-2690585; E-mail: pradip{at}imtech.res.in.

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