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Propeptide processing and proteolytic activity of proenzymes of the Staphylococcal and Enterococcal GluV8-family protease

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Title Propeptide processing and proteolytic activity of proenzymes of the Staphylococcal and Enterococcal GluV8-family protease
 
Creator Rouf, S M A
Ohara-Nemoto, Y
Shimoyama, Y
Kimura, S
Ono, T
Nemoto, T K
 
Subject Enterococcus faecalis
GluV8
Propeptide
Staphylococcus aureus
 
Description 421-427
Proenzymes with
various lengths of propeptides have been observed in GluV8 from Staphylococcus
aureus and GluSE from S. epidermidis. However, the production
mechanism of these proenzymes and roles of truncated propeptides have yet
to be elucidated. Here we demonstrate that shortening of propeptide
commonly occurs in an auto-catalytic manner in
GluV8-family members, including those from coagulase negative Staphylococci and Enterococcus
faecalis. Accompanied with propeptide shortening,
the pro-mature junction (Asn/Ser-1-Val1) becomes more
susceptible towards the hetero-catalytic maturation enzymes. The auto-catalytic propeptide truncation is not observed in Ser169Ala inert molecules of
GluV8-family members. A faint proteolytic activity of
proenzymes from Staphylococcus caprae
and
E. faecalis is detected. In addition,
proteolytic activity of proenzyme of GluV8 carrying Arg-3AlaAsn-1
is demonstrated with synthetic peptide substrates LLE/Q-MCA. These results
suggest that GluV8-family proenzymes with shortened propeptides intrinsically
possess proteolytic activity and are involved in the propeptide shortening that
facilitates the final hetero-catalytic maturation.
 
Date 2012-12-13T07:24:22Z
2012-12-13T07:24:22Z
2012-12
 
Type Article
 
Identifier 0975-0959 (Online); 0301-1208 (Print)
http://hdl.handle.net/123456789/15240
 
Language en_US
 
Rights CC Attribution-Noncommercial-No Derivative Works 2.5 India
 
Publisher NISCAIR-CSIR, India
 
Source IJBB Vol.49(6) [December 2012]