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Journal of Bacteriology, December 2002, p. 6465-6471, Vol. 184, No. 23
0021-9193/02/$04.00+0     DOI: 10.1128/JB.184.23.6465-6471.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Aquifex aeolicus PilT, Homologue of a Surface Motility Protein, Is a Thermostable Oligomeric NTPase

Timothy J. Herdendorf,1 Darrell R. McCaslin,2 and Katrina T. Forest1*

Department of Bacteriology,1 Department of Biochemistry and Biophysical Instrumentation Facility, University of Wisconsin-Madison, Madison, Wisconsin 537062

Received 24 May 2002/ Accepted 30 August 2002

Bacterial surface motility works by retraction of surface-attached type IV pili. This retraction requires the PilT protein, a member of a large family of putative NTPases from type II and IV secretion systems. In this study, the PilT homologue from the thermophilic eubacterium Aquifex aeolicus was cloned, overexpressed, and purified. A. aeolicus PilT was shown to be a thermostable ATPase with a specific activity of 15.7 nmol of ATP hydrolyzed/min/mg of protein. This activity was abolished when a conserved lysine in the nucleotide-binding motif was altered. The substrate specificity was low; UTP, CTP, ATP, GTP, dATP, and dGTP served as substrates, UTP having the highest activity of these in vitro. Based on sedimentation equilibrium and size exclusion chromatography, PilT was identified as a {approx}5- to 6-subunit oligomer. Potential implications of the NTPase activity of PilT in pilus retraction are discussed.

* Corresponding author. Mailing address: Department of Bacteriology, University of Wisconsin, Madison, 1550 Linden Drive, Madison, WI 53706. Phone: (608) 265-3566. Fax: (608) 262-9865. E-mail: forest{at}bact.wisc.edu.

Journal of Bacteriology, December 2002, p. 6465-6471, Vol. 184, No. 23
0021-9193/02/$04.00+0     DOI: 10.1128/JB.184.23.6465-6471.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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