Please use this identifier to cite or link to this item: http://nopr.niscair.res.in/handle/123456789/15240
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: <i style="mso-bidi-font-style:normal"><span style="font-size:9.0pt;font-family:"Times New Roman";mso-fareast-font-family: "Times New Roman";mso-bidi-font-family:Mangal;color:black;mso-ansi-language: EN-GB;mso-fareast-language:EN-US;mso-bidi-language:HI" lang="EN-GB">Enterococcus faecalis</span></i>
GluV8
Propeptide
<i style="mso-bidi-font-style:normal"><span style="font-size:9.0pt;font-family:"Times New Roman";mso-fareast-font-family: "Times New Roman";mso-bidi-font-family:Mangal;color:black;mso-ansi-language: EN-GB;mso-fareast-language:EN-US;mso-bidi-language:HI" lang="EN-GB">Staphylococcus aureus</span></i>
Issue Date: Dec-2012
Publisher: NISCAIR-CSIR, India
Abstract: Proenzymes with various lengths of propeptides have been observed in GluV8 from <i>Staphylococcus aureus </i>and GluSE from <i>S. epidermidis</i>. 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 <i style="mso-bidi-font-style:normal">Staphylococci</i> and <i>Enterococcus faecalis</i>. Accompanied with propeptide shortening, the pro-mature junction (Asn/Ser<sub>-1</sub>-Val<sub>1</sub>) 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 <i style="mso-bidi-font-style:normal">Staphylococcus caprae</i> and <i style="mso-bidi-font-style:normal">E. faecalis</i> is detected. In addition, proteolytic activity of proenzyme of GluV8 carrying Arg<sub>-3</sub>AlaAsn<sub>-1</sub> 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.
Description: 421-427
URI: http://hdl.handle.net/123456789/15240
ISSN: 0975-0959 (Online); 0301-1208 (Print)
Appears in Collections:IJBB Vol.49(6) [December 2012]

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