Prokaryotic histone-like protein interacting with RNA polymerase.
firA mutation of Escherichia coli can render RNA synthesis thermosensitive and confer abnormal sensitivity to rifampicin, an antibiotic that specifically inhibits the activity of RNA polymerase. We previously described the cloning of a chromosomal HindIII fragment containing the firA gene, and we now present strong evidence that the product of this gene is a 17,000-dalton polypeptide which, by various criteria, closely resembles the eukaryotic histones. This protein forms the largest of a unique set of three abundant histone-like proteins (HLP) found in E. coli and is hence referred to as HLPI. We discuss possible routes by which these proteins might affect transcription.
D010582:Bacteriophage lambda; D002874:Chromosome Mapping; D012321:DNA-Directed RNA Polymerases / Q000378:metabolism*; D004352:Drug Resistance, Microbial; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000235:genetics*; D006657:Histones / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D009154:Mutation; D012318:RNA Polymerase I / Q000378:metabolism*; D012293:Rifampin / Q000378:metabolism; D013696:Temperature; D014158:Transcription, Genetic / Q000187:drug effects*; D014161:Transduction, Genetic
D006657:Histones; D012321:DNA-Directed RNA Polymerases; D012318:RNA Polymerase I; D012293:Rifampin