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FlaK of the archaeon Methanococcus maripaludis possesses preflagellin peptidase activity. FEMS Microbiol Lett 2002 Feb 19;208(1):53-9

Date

04/06/2002

Pubmed ID

11934494

DOI

10.1111/j.1574-6968.2002.tb11060.x

Abstract

Archaeal flagellins are initially synthesized as preflagellins with a short, positively charged leader peptide, which is cleaved prior to the incorporation of the mature flagellins into the filament. While preflagellin peptidase activity had previously been detected in methanogen membranes, the enzyme responsible for this activity had not been identified. We show here that FlaK of Methanococcus maripaludis has preflagellin peptidase activity. In an in vitro preflagellin peptidase assay, Escherichia coli membranes overexpressing Methanococcus voltae preflagellin FlaB2 (as substrate) were combined with E. coli membranes overexpressing M. maripaludis FlaK (as enzyme). Cleavage of the preflagellin was demonstrated by immunoblotting using antibody to FlaB2 and detection of a faster migrating cross-reactive species. This activity required detergent in the assay, and was not detected in membranes previously heated to 95 degrees C. This is the first reported identification of the preflagellin peptidase, and aside from the flagellins, this is the first assignment of function to a gene involved in archaeal flagellation.

Author List

Bardy SL, Jarrell KF

Author

Sonia L. Bardy in the Biological Sciences department at University of Wisconsin - Milwaukee




MESH terms used to index this publication - Major topics in bold

Amino Acid Sequence
Archaeal Proteins
Endopeptidases
Escherichia coli
Flagella
Flagellin
Methanococcus
Molecular Sequence Data
Protein Precursors
Sequence Alignment
Sequence Analysis, DNA
jenkins-FCD Prod-482 91ad8a360b6da540234915ea01ff80e38bfdb40a