Prokaryotic histone-like protein interacting with RNA polymerase.

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.