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. 1980 Jun;77(6):3548-52.
doi: 10.1073/pnas.77.6.3548.

Prokaryotic histone-like protein interacting with RNA polymerase

R Lathe, H Buc, J P Lecocq, E K Bautz

Prokaryotic histone-like protein interacting with RNA polymerase

R Lathe et al. Proc Natl Acad Sci U S A. 1980 Jun.

Abstract

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.

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