This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Google Scholar
Right arrow Articles by Ng, S. Y. M.
Right arrow Articles by Jarrell, K. F.
PubMed
Right arrow PubMed Citation
Right arrow Articles by Ng, S. Y. M.
Right arrow Articles by Jarrell, K. F.

 Previous Article  |  Next Article 

Journal of Bacteriology, November 2009, p. 6732-6740, Vol. 191, No. 21
0021-9193/09/$08.00+0     doi:10.1128/JB.00673-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Different Minimal Signal Peptide Lengths Recognized by the Archaeal Prepilin-Like Peptidases FlaK and PibD{triangledown}

Sandy Y. M. Ng,1 David J. VanDyke,1 Bonnie Chaban,1 John Wu,1 Yoshika Nosaka,2 Shin-Ichi Aizawa,2 and Ken F. Jarrell1*

Department of Microbiology and Immunology, Queen's University, Kingston, Ontario, Canada K7L 3N6,1 Department of Life Sciences, Prefectural University of Hiroshima, 562 Nanatsuka, Shobara, Hiroshima 727-0023, Japan2

Received 22 May 2009/ Accepted 23 August 2009

In Archaea, the preflagellin peptidase (a type IV prepilin-like peptidase designated FlaK in Methanococcus voltae and Methanococcus maripaludis) is the enzyme that cleaves the N-terminal signal peptide from preflagellins. In methanogens and several other archaeal species, the typical flagellin signal peptide length is 11 to 12 amino acids, while in other archaea preflagellins possess extremely short signal peptides. A systematic approach to address the signal peptide length requirement for preflagellin processing is presented in this study. M. voltae preflagellin FlaB2 proteins with signal peptides 3 to 12 amino acids in length were generated and used as a substrate in an in vitro assay utilizing M. voltae membranes as an enzyme source. Processing by FlaK was observed in FlaB2 proteins containing signal peptides shortened to 5 amino acids; signal peptides 4 or 3 amino acids in length were unprocessed. In the case of Sulfolobus solfataricus, where the preflagellin peptidase PibD has broader substrate specificity, some predicted substrates have predicted signal peptides as short as 3 amino acids. Interestingly, the shorter signal peptides of the various mutant FlaB2 proteins not processed by FlaK were processed by PibD, suggesting that some archaeal preflagellin peptidases are likely adapted toward cleaving shorter signal peptides. The functional complementation of signal peptidase activity by FlaK and PibD in an M. maripaludis {Delta}flaK mutant indicated that processing of preflagellins was detected by complementation with either FlaK or PibD, yet only FlaK-complemented cells were flagellated. This suggested that a block in an assembly step subsequent to signal peptide removal occurred in the PibD complementation.

* Corresponding author. Mailing address: Department of Microbiology and Immunology, Queen's University, Kingston, Ontario, Canada K7L 3N6. Phone: (613) 533-2456. Fax: (613) 533-6796. E-mail: jarrellk{at}queensu.ca

{triangledown} Published ahead of print on 28 August 2008.

Journal of Bacteriology, November 2009, p. 6732-6740, Vol. 191, No. 21
0021-9193/09/$08.00+0     doi:10.1128/JB.00673-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.





Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»