PMID:1987124
| Citation |
Dicker, IB and Seetharam, S (1991) Cloning and nucleotide sequence of the firA gene and the firA200(Ts) allele from Escherichia coli. J. Bacteriol. 173:334-44 |
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| Abstract |
The Escherichia coli gene firA, previously reported to code for a small, histonelike DNA-binding protein, has been cloned and found to reside immediately downstream from skp, a gene previously identified as the firA locus. firA encodes a 36-kDa protein. The mutant firA200(Ts) allele was also cloned and shown to contain three mutations, each mutation giving rise to a single amino acid change. Partially purified wild-type FirA (from a firA+ strain) and mutant FirA [from a firA200(Ts) strain] proteins have amino-terminal sequences predicted from their common DNA sequences. Both proteins lack an N-terminal methionine. Modest overexpression of wild-type or mutant FirA restored wild-type growth to firA200(Ts) strains at 43 degrees C, whereas high-level expression of wild-type FirA was required for more complete suppression of the rifampin sensitivity of firA200(Ts) rpoB double mutants. High-level expression of mutant FirA did not suppress this rifampin sensitivity. |
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| Keywords |
Amino Acid Sequence; Base Sequence; DNA, Bacterial/genetics; DNA-Binding Proteins/biosynthesis; DNA-Binding Proteins/genetics; DNA-Directed RNA Polymerases/metabolism; Escherichia coli/genetics; Escherichia coli/growth & development; Escherichia coli/metabolism; Genes, Bacterial; Genetic Vectors; Genotype; Kinetics; Methionine; Molecular Sequence Data; Protein Biosynthesis; Restriction Mapping; Software; Transcription, Genetic |
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