Different minimal signal peptide lengths recognized by the archaeal prepilin-like peptidases FlaK and PibD

S Y M Ng; D J VanDyke; Bonnie L Chaban; John Wu; Y Nosaka; S I Aizawa; K F Jarrell

doi:10.1128/JB.00673-09

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Different minimal signal peptide lengths recognized by the archaeal prepilin-like peptidases FlaK and PibD

Journal article

Peer reviewed

Different minimal signal peptide lengths recognized by the archaeal prepilin-like peptidases FlaK and PibD

S Y M Ng, D J VanDyke, Bonnie L Chaban, John Wu, Y Nosaka, S I Aizawa and K F Jarrell

Journal of Bacteriology, Vol.191(21), pp.6732-6740

2009

DOI: https://doi.org/10.1128/JB.00673-09

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Abstract

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 ΔflaK 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. Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Details

Title: Different minimal signal peptide lengths recognized by the archaeal prepilin-like peptidases FlaK and PibD
Authors: S Y M Ng (Author) - Queen's University, Canada
D J VanDyke (Author) - Queen's University, Canada
Bonnie L Chaban (Author) - Queen's University, Canada
John Wu (Author) - Queen's University, Canada
Y Nosaka (Author) - Prefectural University of Hiroshima, Japan
S I Aizawa (Author) - Prefectural University of Hiroshima, Japan
K F Jarrell (Author) - Queen's University, Canada
Publication details: Journal of Bacteriology, Vol.191(21), pp.6732-6740
Publisher: American Society for Microbiology
Date published: 2009
DOI: 10.1128/JB.00673-09
ISSN: 0021-9193
Organisation Unit: University of the Sunshine Coast, Queensland; Thompson Institute; Centre for Bioinnovation
Language: English
Record Identifier: 99450805802621
Output Type: Journal article

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Web Of Science research areas: Microbiology

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