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PMID: 6447875 Published · ppublish English Journal Article

Prokaryotic histone-like protein interacting with RNA polymerase.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 77 ·No. 6 ·1980-06-00 ·Pages 3548-52

Lathe R, Buc H, Lecocq JP, Bautz EK

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.

MeSH Terms
Bacteriophage lambda Chromosome Mapping DNA-Directed RNA Polymerases/metabolism Drug Resistance, Microbial Electrophoresis, Polyacrylamide Gel Escherichia coli/genetics Histones/genetics,isolation & purification,metabolism Mutation RNA Polymerase I/metabolism Rifampin/metabolism Temperature Transcription, Genetic/drug effects Transduction, Genetic
Chemicals
Histones DNA-Directed RNA Polymerases RNA Polymerase I Rifampin
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Lathe R
Buc H
Lecocq J P
Bautz E K
References (28)
28 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.77.6.3548
Published
1980-06-00
Pages
3548-52
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC349654
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.77.6.3548 PMC Full Text View journal details
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