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 Szabó, Z. Articles by Driessen, A. J. M. Search for Related Content PubMed PubMed Citation Articles by Szabó, Z. Articles by Driessen, A. J. M.

 Previous Article  |  Next Article 

Journal of Bacteriology, February 2006, p. 1437-1443, Vol. 188, No. 4
0021-9193/06/$08.00+0     doi:10.1128/JB.188.4.1437-1443.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Active-Site Residues in the Type IV Prepilin Peptidase Homologue PibD from the Archaeon Sulfolobus solfataricus

Department of Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Kerklaan 30, 9751 NN Haren, The Netherlands

Received 28 October 2005/ Accepted 30 November 2005

Archaeal preflagellin peptidases and bacterial type IV prepilin peptidases belong to a family of aspartic acid proteases that cleave the leader peptides of precursor proteins with type IV prepilin signal sequences. The substrate repertoire of PibD from the crenarchaeon Sulfolobus solfataricus is unusually diverse. In addition to flagellin, PibD cleaves three sugar-binding proteins unique to this species and a number of proteins with unknown function. Here we demonstrate that PibD contains two aspartic acid residues that are essential for cleavage activity. An additional pair of aspartic acids in a large cytoplasmic loop is also important for function and is possibly involved in leader peptide recognition. Combining the results of transmembrane segment predictions and cysteine-labeling experiments, we suggest a membrane topology model for PibD with the active-site aspartic acid residues exposed to the cytosol.

This article has been cited by other articles:

• Ng, S. Y. M., Zolghadr, B., Driessen, A. J. M., Albers, S.-V., Jarrell, K. F. (2008). Cell Surface Structures of Archaea. J. Bacteriol. 190: 6039-6047 [Full Text]  
• Szabo, Z., Sani, M., Groeneveld, M., Zolghadr, B., Schelert, J., Albers, S.-V., Blum, P., Boekema, E. J., Driessen, A. J. M. (2007). Flagellar Motility and Structure in the Hyperthermoacidophilic Archaeon Sulfolobus solfataricus. J. Bacteriol. 189: 4305-4309 [Abstract] [Full Text]  
• Ng, S. Y. M., Chaban, B., VanDyke, D. J., Jarrell, K. F. (2007). Archaeal signal peptidases. Microbiology 153: 305-314 [Abstract] [Full Text]  
• Szabo, Z., Stahl, A. O., Albers, S.-V., Kissinger, J. C., Driessen, A. J. M., Pohlschroder, M. (2007). Identification of Diverse Archaeal Proteins with Class III Signal Peptides Cleaved by Distinct Archaeal Prepilin Peptidases. J. Bacteriol. 189: 772-778 [Abstract] [Full Text]  
• Tomich, M., Fine, D. H., Figurski, D. H. (2006). The TadV Protein of Actinobacillus actinomycetemcomitans Is a Novel Aspartic Acid Prepilin Peptidase Required for Maturation of the Flp1 Pilin and TadE and TadF Pseudopilins.. J. Bacteriol. 188: 6899-6914 [Abstract] [Full Text]  
• de Bentzmann, S., Aurouze, M., Ball, G., Filloux, A. (2006). FppA, a Novel Pseudomonas aeruginosa Prepilin Peptidase Involved in Assembly of Type IVb Pili. J. Bacteriol. 188: 4851-4860 [Abstract] [Full Text]