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Journal of Bacteriology, February 2001, p. 1482-1488, Vol. 183, No. 4
Laboratoire de Microbiologie de
l'Environnement, IRBA, Université de Caen, 14032 Caen Cedex,
France
Received 28 August 2000/Accepted 1 November 2000
The Enterococcus faecalis general stress protein Gsp65
has been purified from two-dimensional gel electrophoresis.
Determination of its N-terminal sequence and characterization of the
corresponding gene revealed that the gsp65 product is a
133-amino-acid protein sharing homologies with organic hydroperoxide
resistance (Ohr) proteins. Transcriptional analysis of
gsp65 gave evidence for a monocistronic mRNA initiated 52 nucleotides upstream of the ATG start codon and for an induction in
response to hydrogen peroxide, heat shock, acid pH, detergents,
ethanol, sodium chloride, and tert-butylhydroperoxide
(tBOOH). A gsp65 mutant showed increased sensitivity to the
organic hydroperoxide tBOOH and to ethanol.
0021-9193/01/$04.00+0 DOI: 10.1128/JB.183.4.1482-1488.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
Identification and Characterization of
gsp65, an Organic Hydroperoxide Resistance (ohr)
Gene Encoding a General Stress Protein in Enterococcus
faecalis
and
*
Corresponding author. Mailing address: Laboratoire de
Microbiologie de l'Environnement, IRBA, Université de Caen,
14032 Caen Cedex, France. Phone: 00-33-2-31-56-55-23. Fax
00-33-2-31-56-53-11. E.mail: rince{at}ibba.unicaen.fr.
Present address: Laboratoire de Biologie Cellulaire et
Moléculaire, Université du Littoral-Côte d'Opale,
62327 Boulogne sur Mer Cedex, France.
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