Literature DB >> 9931440

Identification and molecular characterization of a gene homologous to epr (endopeptidase resistance gene) in Staphylococcus aureus.

M Sugai1, T Fujiwara, H Komatsuzawa.   

Abstract

Certain Staphylococci possess a gene called epr or lif that renders the cells resistant to lysis by glycylglycine endopeptidase. The resistance is conferred by modifying the amino acid composition of interpeptide chains in cell-wall peptidoglycan by increasing serine content and decreasing glycine content. A gene homologous to epr/lif was cloned from S. aureus RN450 genomic libraries and designated eprh. eprh was found to localize 27bp downstream of a novel cell-wall hydrolase gene lytN, which is in the same orientation with eprh. By analogy with epr/lif, eprh is suggested to be involved in the transfer of certain amino acids, possibly serine or amino acids other than glycine, to interpeptide chains of cell-wall peptidoglycan. Unlike epr/lif, overexpression of eprh in S. aureus did not result in an increased resistance to lysostaphin. Insertional inactivation of eprh or lytN by Campbell-type integration did not affect the susceptibility of the cells to lysostaphin, either. These results suggest that eprh and lytN are not essential genes for S. aureus growth. The physiological function of eprh remains unknown.

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Year:  1998        PMID: 9931440     DOI: 10.1016/s0378-1119(98)00508-3

Source DB:  PubMed          Journal:  Gene        ISSN: 0378-1119            Impact factor:   3.688


  21 in total

Review 1.  FemABX peptidyl transferases: a link between branched-chain cell wall peptide formation and beta-lactam resistance in gram-positive cocci.

Authors:  S Rohrer; B Berger-Bächi
Journal:  Antimicrob Agents Chemother       Date:  2003-03       Impact factor: 5.191

2.  Cell wall composition and decreased autolytic activity and lysostaphin susceptibility of glycopeptide-intermediate Staphylococcus aureus.

Authors:  Jennifer L Koehl; Arunachalam Muthaiyan; Radheshyam K Jayaswal; Kerstin Ehlert; Harald Labischinski; Brian J Wilkinson
Journal:  Antimicrob Agents Chemother       Date:  2004-10       Impact factor: 5.191

3.  Transcriptomic and functional analysis of an autolysis-deficient, teicoplanin-resistant derivative of methicillin-resistant Staphylococcus aureus.

Authors:  Adriana Renzoni; Christine Barras; Patrice François; Yvan Charbonnier; Elzbieta Huggler; Christian Garzoni; William L Kelley; Paul Majcherczyk; Jacques Schrenzel; Daniel P Lew; Pierre Vaudaux
Journal:  Antimicrob Agents Chemother       Date:  2006-09       Impact factor: 5.191

4.  Conditional mutation of an essential putative glycoprotease eliminates autolysis in Staphylococcus aureus.

Authors:  Li Zheng; Chuanxin Yu; Kenneth Bayles; Iñigo Lasa; Yinduo Ji
Journal:  J Bacteriol       Date:  2007-01-19       Impact factor: 3.490

5.  LytN, a murein hydrolase in the cross-wall compartment of Staphylococcus aureus, is involved in proper bacterial growth and envelope assembly.

Authors:  Matthew B Frankel; Antoni P A Hendrickx; Dominique M Missiakas; Olaf Schneewind
Journal:  J Biol Chem       Date:  2011-07-22       Impact factor: 5.157

Review 6.  Bacterial proteases: targets for diagnostics and therapy.

Authors:  W E Kaman; J P Hays; H P Endtz; F J Bikker
Journal:  Eur J Clin Microbiol Infect Dis       Date:  2014-02-18       Impact factor: 3.267

7.  Genome-wide analysis of ruminant Staphylococcus aureus reveals diversification of the core genome.

Authors:  Nouri L Ben Zakour; Daniel E Sturdevant; Sergine Even; Caitriona M Guinane; Corinne Barbey; Priscila D Alves; Marie-Françoise Cochet; Michel Gautier; Michael Otto; J Ross Fitzgerald; Yves Le Loir
Journal:  J Bacteriol       Date:  2008-06-20       Impact factor: 3.490

8.  Perturbation of cell wall synthesis suppresses autolysis in Staphylococcus aureus: evidence for coregulation of cell wall synthetic and hydrolytic enzymes.

Authors:  Aude Antignac; Krzysztof Sieradzki; Alexander Tomasz
Journal:  J Bacteriol       Date:  2007-09-07       Impact factor: 3.490

9.  Identification of the Staphylococcus aureus etd pathogenicity island which encodes a novel exfoliative toxin, ETD, and EDIN-B.

Authors:  Takayuki Yamaguchi; Koji Nishifuji; Megumi Sasaki; Yasuyuki Fudaba; Martin Aepfelbacher; Takashi Takata; Masaru Ohara; Hitoshi Komatsuzawa; Masayuki Amagai; Motoyuki Sugai
Journal:  Infect Immun       Date:  2002-10       Impact factor: 3.441

10.  FmhA and FmhC of Staphylococcus aureus incorporate serine residues into peptidoglycan cross-bridges.

Authors:  Stephanie Willing; Emma Dyer; Olaf Schneewind; Dominique Missiakas
Journal:  J Biol Chem       Date:  2020-08-05       Impact factor: 5.157

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