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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred


IMPACT FACTOR 2018: 3.014
5-year IMPACT FACTOR: 3.162

CiteScore 2018: 3.09

SCImago Journal Rank (SJR) 2018: 1.482
Source Normalized Impact per Paper (SNIP) 2018: 0.820

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1437-4315
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Volume 389, Issue 9

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Homologous and heterologous expression and maturation processing of extracellular glutamyl endopeptidase of Staphylococcus epidermidis

Yuko Ohara-Nemoto
  • 1Department of Oral Molecular Biology, Course of Medical and Dental Sciences, Nagasaki University Graduate School of Biomedical Sciences, 1-7-1 Sakamoto, Nagasaki 852-8588, Japan
  • Other articles by this author:
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/ Toshio Ono
  • 2Department of Oral Molecular Biology, Course of Medical and Dental Sciences, Nagasaki University Graduate School of Biomedical Sciences, 1-7-1 Sakamoto, Nagasaki 852-8588, Japan
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Yu Shimoyama
  • 3Department of Oral Microbiology, Iwate Medical University School of Dentistry, 1-3-27 Chuodori, Morioka 020-8505, Japan
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/ Shigenobu Kimura
  • 4Department of Oral Microbiology, Iwate Medical University School of Dentistry, 1-3-27 Chuodori, Morioka 020-8505, Japan
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  • De Gruyter OnlineGoogle Scholar
/ Takayuki K. Nemoto
  • 5Department of Oral Molecular Biology, Course of Medical and Dental Sciences, Nagasaki University Graduate School of Biomedical Sciences, 1-7-1 Sakamoto, Nagasaki 852-8588, Japan
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
Published Online: 2008-08-19 | DOI: https://doi.org/10.1515/BC.2008.137

Abstract

The extracellular serine endopeptidase GluSE (EC 3.4.21.19) is considered to be one of the virulence factors of Staphylococcus epidermidis. The present study investigated maturation processing of native GluSE and that heterologously expressed in Escherichia coli. In addition to the 28-kDa mature protease, small amounts of proenzymes with molecular masses of 32, 30, and 29 kDa were identified in the extracellular and cell wall-associated fractions. We defined the pre (M1-A27)- and pro (K28-S66)-segments, and found that processing at the E32-S33 and D48-I49 bonds was responsible for production of the 30- and 29-kDa intermediates, respectively. The full-length form of C-terminally His-tagged GluSE was purified as three proenzymes equivalent to the native ones. These molecules possessing an entire or a part of the pro-segment were proteolytically latent and converted to a mature 28-kDa form by thermolysin cleavage at the S66-V67 bond. Mutation of the essential amino acid S235 suggested auto-proteolytic production of the 30- and 29-kDa intermediates. Furthermore, an undecapeptide (I56-S66) of the truncated pro-segment not only functions as an inhibitor of the protease but also facilitates thermolysin processing. These findings could offer clues to the molecular mechanism involved in the regulation of proteolytic activity of pathogenic proteases secreted from S. epidermidis.

Keywords: prepro-segment; recombinant protein; signal sequence; Staphylococcus epidermidis; thermolysin; V8 protease

About the article

Corresponding author


Received: 2007-10-02

Accepted: 2008-04-01

Published Online: 2008-08-19

Published in Print: 2008-09-01


Citation Information: Biological Chemistry, Volume 389, Issue 9, Pages 1209–1217, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2008.137.

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