Prokaryotic histone-like protein interacting with RNA polymerase.

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Abstract
FirA mutations of Escherichia coli can render RNA synthesis thermosensitive and confer abnormal sensitivity to rifampicin, an antibiotic that specifically inhibits the activity of RNA polymerase. The cloning of a chromosomal HindIII fragment containing the firA gene was described previously, and now strong evidence that the product of this gene is a 17,000 dalton polypeptide which, by various criteria, closely resembles the eukaryotic histones is presented. This protein forms the largest of a unique set of 3 abundant histone-like proteins (HLP) found in E. coli and is hence referred to as HLPI. Possible routes by which these proteins might affect transcription were discussed.