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Journal of Bacteriology, April 2009, p. 2307-2314, Vol. 191, No. 7
0021-9193/09/$08.00+0     doi:10.1128/JB.01353-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Properties of HflX, an Enigmatic Protein from Escherichia coli{triangledown}

Dipak Dutta,1,{dagger} Kaustav Bandyopadhyay,1 Ajit Bikram Datta,1,{ddagger} Abhijit A. Sardesai,2 and Pradeep Parrack1*

Department of Biochemistry, Bose Institute, P-1/12, C.I.T. Scheme VIIM, Kolkata 700054, India,1 Centre for DNA Fingerprinting and Diagnostics, Hyderabad 500076, India2

Received 29 September 2008/ Accepted 7 January 2009

The Escherichia coli gene hflX was first identified as part of the hflA operon, mutations in which led to an increased frequency of lysogenization upon infection of the bacterium by the temperate coliphage lambda. Independent mutational studies have also indicated that the HflX protein has a role in transposition. Based on the sequence of its gene, HflX is predicted to be a GTP-binding protein, very likely a GTPase. We report here purification and characterization of the HflX protein. We also specifically examined its suggested functional roles mentioned above. Our results show that HflX is a monomeric protein with a high (30% to 40%) content of helices. It exhibits GTPase as well as ATPase activities, but it has no role in lambda lysogeny or in transposition.

* Corresponding author. Mailing address: Department of Biochemistry, Bose Institute, P-1/12, C.I.T. Scheme VIIM, Kolkata 700054, India. Phone: 91-33-25693227. Fax: 91-33-23553886. E-mail: pradeep{at}bic.boseinst.ernet.in

{triangledown} Published ahead of print on 30 January 2009.

{dagger} Present address: New York University School of Medicine, Smilow Research Center, New York, NY 10016.

{ddagger} Present address: Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205.

Journal of Bacteriology, April 2009, p. 2307-2314, Vol. 191, No. 7
0021-9193/09/$08.00+0     doi:10.1128/JB.01353-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.





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