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Research Journals >
Indian Journal of Biochemistry and Biophysics (IJBB) >
IJBB Vol.49 [2012] >
IJBB Vol.49(6) [December 2012] >
| Title: | Propeptide processing and proteolytic activity of proenzymes of the Staphylococcal and Enterococcal GluV8-family protease |
| Authors: | Rouf, S M A
Ohara-Nemoto, Y
Shimoyama, Y
Kimura, S
Ono, T
Nemoto, T K |
| Keywords: | Enterococcus faecalis
GluV8
Propeptide
Staphylococcus aureus |
| Issue Date: | Dec-2012 |
| Publisher: | NISCAIR-CSIR, India |
| Abstract: | 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. |
| Page(s): | 421-427 |
| CC License: |  CC Attribution-Noncommercial-No Derivative Works 2.5 India |
| ISSN: | 0975-0959 (Online); 0301-1208 (Print) |
| Source: | IJBB Vol.49(6) [December 2012]
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