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J Biol Chem, Vol. 275, Issue 2, 1502-1510, January 14, 2000
From the Department of Microbiology, Dartmouth Medical School,
Hanover, New Hampshire 03755
Type 4 prepilins or prepilin-like-proteins are
secreted by a wide range of bacterial species and are required for a
variety of functions including type 4 pilus formation, toxin and other enzyme secretion, gene transfer, and biofilm formation. A distinctive feature of these proteins is the presence of a specialized leader peptide that is cleaved off by a cognate membrane-bound type 4 prepilin
peptidase (TFPP) during the process of secretion. In this report we
show that the TFPPs represent a novel family of bilobed aspartate
proteases that is unlike any other protease. The active site pairs of
aspartic acids of the two TFPPs in Vibrio cholerae are
found at positions 125 and 189 of TcpJ and 147 and 212 of VcpD.
Corresponding aspartate residues are completely conserved throughout
this extensive peptidase family.
The Type 4 Prepilin Peptidases Comprise a Novel Family of
Aspartic Acid Proteases*
and
*
This work was supported in part by Grant ROI AI 23096 from
the National Institutes of Health.The costs of publication of this article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Recipient of Predoctoral Fellowship AI F31-09635 from the National
Institutes of Health.
§
To whom correspondence should be addressed: Dept. of Microbiology,
Dartmouth Medical School, Hanover, NH 03755. Tel.: 603-650-1632; Fax:
603-650-1318; E-mail: ronald.k.taylor@dartmouth.edu.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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