PMID:1592821
| Citation |
Collins, LA, Egan, SM and Stewart, V (1992) Mutational analysis reveals functional similarity between NARX, a nitrate sensor in Escherichia coli K-12, and the methyl-accepting chemotaxis proteins. J. Bacteriol. 174:3667-75 |
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| Abstract |
During anaerobic growth, nitrate induces synthesis of the anaerobic respiratory enzymes formate dehydrogenase-N and nitrate reductase. This induction is mediated by a transcription activator, the narL gene product. The narX gene product may be involved in sensing nitrate and phosphorylating NARL. We isolated narX mutants, designated narX*, that caused nitrate-independent expression of the formate dehydrogenase-N and nitrate reductase structural genes. We used lambda narX specialized transducing phage to genetically analyze these lesions in single copy. Two previously isolated narX* mutations, narX32 and narX71, were also constructed by site-specific mutagenesis. We found that each of these alleles caused nitrate-independent synthesis of formate dehydrogenase-N and nitrate reductase, and each was recessive to narX+. The narX* mutations lie in a region of similarity with the methyl-accepting chemotaxis protein Tsr. We suggest that the narX* proteins have lost a transmembrane signalling function such that phosphoprotein phosphatase activity is reduced relative to protein kinase activity. |
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| Keywords |
Amino Acid Sequence; Bacterial Proteins/genetics; Base Sequence; DNA Mutational Analysis; Escherichia coli/genetics; Escherichia coli Proteins; Gene Expression Regulation, Bacterial/drug effects; Gene Expression Regulation, Bacterial/genetics; Genetic Complementation Test; Membrane Proteins/genetics; Molecular Sequence Data; Molybdenum/pharmacology; Mutagenesis; Mutation/genetics; Nitrates/pharmacology; Phenotype; Protein Kinases; Sequence Alignment/methods; Sequence Homology, Nucleic Acid; Signal Transduction/drug effects; Signal Transduction/genetics |
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