Identification and Functional Characterization of a Xenorhabdus nematophila Oligopeptide Permease
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چکیده
منابع مشابه
Identification and functional characterization of a Xenorhabdus nematophila oligopeptide permease.
The bacterium Xenorhabdus nematophila is a mutualist of Steinernema carpocapsae nematodes and a pathogen of insects. Presently, it is not known what nutrients the bacterium uses to thrive in these host environments. In other symbiotic bacteria, oligopeptide permeases have been shown to be important in host interactions, and we therefore sought to determine if oligopeptide uptake is essential fo...
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T he gram-negative bacterium Xenorhabdus nematophila engages in a mutualistic relationship with a specific soil nematode and also can mount potent pathogenic attacks on a variety of insects. During its mutualisticpathogenic life cycle, Xenorhabdus produces a wide range of exoenzymes, antimicrobial and nematicidal compounds, and insect toxins. Moreover, the nematode-bacteria complex is useful fo...
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We describe purification and characterization of an oligopeptide permease protein (Hly-OppA) from Vibrio furnissii that has multifaceted functions in solute binding, in in vitro hemolysis, in antibiotic resistance, and as a virulence factor in bacterial pathogenesis. The solute-binding function was revealed by N-terminal and internal peptide sequences of the purified protein and was confirmed b...
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We describe a two-gene cluster encoding a bacteriocin, xenocin, and the cognate immunity protein in the insect-pathogenic bacterium Xenorhabdus nematophila, which infects and kills larval stages of the common crop pest Helicoverpa armigera. The two genes, xcinA and ximB, are present in the genome as a single transcriptional unit, which is regulated under SOS conditions. The stress-inducible pro...
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The symbiotic pathogenic bacterium Xenorhabdus nematophila produces two distinct intracellular inclusion bodies. The pixA gene, which encodes the 185-residue methionine-rich PixA inclusion body protein, was analyzed in the present study. The pixA gene was optimally expressed under stationary-phase conditions but its expression did not require RpoS. Analysis of a pixA mutant strain showed that P...
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ژورنال
عنوان ژورنال: Applied and Environmental Microbiology
سال: 2004
ISSN: 0099-2240,1098-5336
DOI: 10.1128/aem.70.9.5621-5627.2004