This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Herdendorf, T. J. Articles by Forest, K. T. Search for Related Content PubMed PubMed Citation Articles by Herdendorf, T. J. Articles by Forest, K. T.

 Previous Article  |  Next Article 

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

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 5- to 6-subunit oligomer. Potential implications of the NTPase activity of PilT in pilus retraction are discussed.

This article has been cited by other articles:

• Chakraborty, S., Monfett, M., Maier, T. M., Benach, J. L., Frank, D. W., Thanassi, D. G. (2008). Type IV Pili in Francisella tularensis: Roles of pilF and pilT in Fiber Assembly, Host Cell Adherence, and Virulence. Infect. Immun. 76: 2852-2861 [Abstract] [Full Text]  
• Jakovljevic, V., Leonardy, S., Hoppert, M., Sogaard-Andersen, L. (2008). PilB and PilT Are ATPases Acting Antagonistically in Type IV Pilus Function in Myxococcus xanthus. J. Bacteriol. 190: 2411-2421 [Abstract] [Full Text]  
• Chiang, P., Sampaleanu, L. M., Ayers, M., Pahuta, M., Howell, P. L., Burrows, L. L. (2008). Functional role of conserved residues in the characteristic secretion NTPase motifs of the Pseudomonas aeruginosa type IV pilus motor proteins PilB, PilT and PilU. Microbiology 154: 114-126 [Abstract] [Full Text]  
• Higashi, D. L., Lee, S. W., Snyder, A., Weyand, N. J., Bakke, A., So, M. (2007). Dynamics of Neisseria gonorrhoeae Attachment: Microcolony Development, Cortical Plaque Formation, and Cytoprotection. Infect. Immun. 75: 4743-4753 [Abstract] [Full Text]  
• Collins, R. F., Saleem, M., Derrick, J. P. (2007). Purification and Three-Dimensional Electron Microscopy Structure of the Neisseria meningitidis Type IV Pilus Biogenesis Protein PilG. J. Bacteriol. 189: 6389-6396 [Abstract] [Full Text]  
• Evans, K. J., Lambert, C., Sockett, R. E. (2007). Predation by Bdellovibrio bacteriovorus HD100 Requires Type IV Pili. J. Bacteriol. 189: 4850-4859 [Abstract] [Full Text]  
• Nakasugi, K., Alexova, R., Svenson, C. J., Neilan, B. A. (2007). Functional Analysis of PilT from the Toxic Cyanobacterium Microcystis aeruginosa PCC 7806. J. Bacteriol. 189: 1689-1697 [Abstract] [Full Text]  
• Saarimaa, C., Peltola, M., Raulio, M., Neu, T. R., Salkinoja-Salonen, M. S., Neubauer, P. (2006). Characterization of Adhesion Threads of Deinococcus geothermalis as Type IV Pili.. J. Bacteriol. 188: 7016-7021 [Abstract] [Full Text]  
• Crowther, L. J., Yamagata, A., Craig, L., Tainer, J. A., Donnenberg, M. S. (2005). The ATPase Activity of BfpD Is Greatly Enhanced by Zinc and Allosteric Interactions with Other Bfp Proteins. J. Biol. Chem. 280: 24839-24848 [Abstract] [Full Text]  
• Collins, R. F., Frye, S. A., Balasingham, S., Ford, R. C., Tonjum, T., Derrick, J. P. (2005). Interaction with Type IV Pili Induces Structural Changes in the Bacterial Outer Membrane Secretin PilQ. J. Biol. Chem. 280: 18923-18930 [Abstract] [Full Text]  
• Albers, S.-V., Driessen, A. J. M. (2005). Analysis of ATPases of putative secretion operons in the thermoacidophilic archaeon Sulfolobus solfataricus. Microbiology 151: 763-773 [Abstract] [Full Text]  
• Chiang, P., Habash, M., Burrows, L. L. (2005). Disparate Subcellular Localization Patterns of Pseudomonas aeruginosa Type IV Pilus ATPases Involved in Twitching Motility. J. Bacteriol. 187: 829-839 [Abstract] [Full Text]  
• Aukema, K. G., Kron, E. M., Herdendorf, T. J., Forest, K. T. (2005). Functional Dissection of a Conserved Motif within the Pilus Retraction Protein PilT. J. Bacteriol. 187: 611-618 [Abstract] [Full Text]  
• Camberg, J. L., Sandkvist, M. (2005). Molecular Analysis of the Vibrio cholerae Type II Secretion ATPase EpsE. J. Bacteriol. 187: 249-256 [Abstract] [Full Text]  
• Szczepanowski, R., Krahn, I., Linke, B., Goesmann, A., Puhler, A., Schluter, A. (2004). Antibiotic multiresistance plasmid pRSB101 isolated from a wastewater treatment plant is related to plasmids residing in phytopathogenic bacteria and carries eight different resistance determinants including a multidrug transport system. Microbiology 150: 3613-3630 [Abstract] [Full Text]  
• Maier, B., Koomey, M., Sheetz, M. P. (2004). A force-dependent switch reverses type IV pilus retraction. Proc. Natl. Acad. Sci. USA 101: 10961-10966 [Abstract] [Full Text]  
• Sexton, J. A., Pinkner, J. S., Roth, R., Heuser, J. E., Hultgren, S. J., Vogel, J. P. (2004). The Legionella pneumophila PilT Homologue DotB Exhibits ATPase Activity That Is Critical for Intracellular Growth. J. Bacteriol. 186: 1658-1666 [Abstract] [Full Text]