Autoinducer-2-Producing Protein LuxS, a Novel Salt- and Chloride-Induced Protein in the Moderately Halophilic Bacterium Halobacillus halophilus
Author(s) -
Xaver Sewald,
Stephan H. Saum,
Peter Palm,
Friedhelm Pfeiffer,
Dieter Oesterhelt,
Volker Müller
Publication year - 2007
Publication title -
applied and environmental microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.552
H-Index - 324
eISSN - 1070-6291
pISSN - 0099-2240
DOI - 10.1128/aem.01625-06
Subject(s) - autoinducer , halophile , operon , quorum sensing , homoserine , biochemistry , chemistry , biology , bacteria , gene , escherichia coli , genetics , virulence
The moderately halophilic bacterium Halobacillus halophilus carries a homologue of LuxS, a protein involved in the activated methyl cycle and the production of autoinducer-2, which mediates quorum sensing between certain species. luxS of H. halophilus is part of an operon that encodes an S-adenosylmethionine-dependent methyltransferase, a cysteine synthase, and a beta-cystathionine lyase. Expression of luxS was growth phase dependent, with maximal expression in the mid-exponential growth phase. In addition, transcription of luxS was strictly salt dependent; maximal mRNA concentrations were observed with 2.0 M NaCl in the growth medium. Chloride ions stimulated luxS transcription by a factor of three. Western blot analyses demonstrated a growth phase- and salinity-dependent production of LuxS. Moreover, cellular LuxS levels were strictly chloride dependent. Maximal accumulation of LuxS was observed at 0.5 to 1.0 M Cl(-) and depended on the salinity.
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