Cloning and characterization of a Na+/H+ antiporter gene of the moderately halophilic bacterium Halobacillus aidingensis AD-6T

A gene encoding a Na + /H + antiporter was obtained from the genome of Halobacillus aidingensis AD-6 T , which was sequenced and designated as nhaH . The deduced amino acid sequence of the gene was 91% identical to the NhaH of H. dabanensis , and shared 54% identity with the NhaG of Bacillus subtili...

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Bibliographic Details
Published in:The journal of microbiology 2008, 46(4), , pp.415-421
Main Authors: Zou, Ya Jie, Yang, Li Fu, Wang, Lei, Yang, Su Sheng
Format: Article
Language:English
Subjects:
Agriculture
Amino Acid Sequence
Amino acids
Bacillaceae - chemistry
Bacillaceae - genetics
Bacillaceae - metabolism
Bacteria
Bacterial Proteins - chemistry
Bacterial Proteins - genetics
Bacterial Proteins - metabolism
Base Sequence
Biomedical and Life Sciences
Cell Membrane - chemistry
Cell Membrane - genetics
Cell Membrane - metabolism
Cloning
Cloning, Molecular
E coli
Escherichia coli - genetics
Escherichia coli - metabolism
Labeling
Life Sciences
Microbiology
Molecular Sequence Data
Physiology
Sequence Alignment
Sequence Deletion
Signal transduction
Sodium chloride
Sodium Chloride - metabolism
Sodium-Hydrogen Exchangers - chemistry
Sodium-Hydrogen Exchangers - genetics
Sodium-Hydrogen Exchangers - metabolism
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Summary:A gene encoding a Na + /H + antiporter was obtained from the genome of Halobacillus aidingensis AD-6 T , which was sequenced and designated as nhaH . The deduced amino acid sequence of the gene was 91% identical to the NhaH of H. dabanensis , and shared 54% identity with the NhaG of Bacillus subtilis . The cloned gene enable the Escherichia coli KNabc cell, which lack all of the major Na + /H + antiporters, to grow in medium containing 0.2 M NaCl or 10 mM LiCl. The nhaH gene was predicted to encode a 43.5 kDa protein (403 amino acid residues) with 11 putative transmembrane regions. Everted membrane vesicles prepared from E. coli KNabc cells carrying NhaH exhibited Na + /H + as well as Li + /H + antiporter activity, which was pH-dependent with the highest activity at pH 8.0, and no K + /H + antiporter activity was detected. The deletion of hydrophilic C-terminal amino acid residues showed that the short C-terminal tail was vital for Na + /H + antiporter activity.
ISSN:1225-8873
1976-3794
DOI:10.1007/s12275-008-0009-2