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

Sandy Y.M. Ng, David J. VanDyke, Bonnie Chaban, John Wu, Yoshika Nosaka, Shin Ichi Aizawa, Ken F. Jarrell

研究成果: 雜誌貢獻文章

23 引文 (Scopus)

摘要

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.
原文英語
頁(從 - 到)6732-6740
頁數9
期刊Journal of Bacteriology
191
發行號21
DOIs
出版狀態已發佈 - 十一月 1 2009
對外發佈Yes

指紋

Protein Sorting Signals
Peptide Hydrolases
Amino Acids
Methanococcus
Archaea
Sulfolobus solfataricus
Flagellin
Mutant Proteins
Enzymes
Substrate Specificity
Proteins
preflagellin
Membranes

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology

引用此文

Ng, S. Y. M., VanDyke, D. J., Chaban, B., Wu, J., Nosaka, Y., Aizawa, S. I., & Jarrell, K. F. (2009). Different minimal signal peptide lengths recognized by the archaeal prepilin-like peptidases FlaK and PibD. Journal of Bacteriology, 191(21), 6732-6740. https://doi.org/10.1128/JB.00673-09

Different minimal signal peptide lengths recognized by the archaeal prepilin-like peptidases FlaK and PibD. / Ng, Sandy Y.M.; VanDyke, David J.; Chaban, Bonnie; Wu, John; Nosaka, Yoshika; Aizawa, Shin Ichi; Jarrell, Ken F.

於: Journal of Bacteriology, 卷 191, 編號 21, 01.11.2009, p. 6732-6740.

研究成果: 雜誌貢獻文章

Ng, SYM, VanDyke, DJ, Chaban, B, Wu, J, Nosaka, Y, Aizawa, SI & Jarrell, KF 2009, 'Different minimal signal peptide lengths recognized by the archaeal prepilin-like peptidases FlaK and PibD', Journal of Bacteriology, 卷 191, 編號 21, 頁 6732-6740. https://doi.org/10.1128/JB.00673-09
Ng, Sandy Y.M. ; VanDyke, David J. ; Chaban, Bonnie ; Wu, John ; Nosaka, Yoshika ; Aizawa, Shin Ichi ; Jarrell, Ken F. / Different minimal signal peptide lengths recognized by the archaeal prepilin-like peptidases FlaK and PibD. 於: Journal of Bacteriology. 2009 ; 卷 191, 編號 21. 頁 6732-6740.
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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.",
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