PpGpp regulates the binding of two RNA polymerase molecules to the tyrT promoter.

Nucleic acids research ·Vol. 10 ·No. 16 ·1982-08-25 ·Pages 5043-57

Travers AA, Lamond AI, Mace HA

Abstract

Bacterial promoters differ in the number of RNA polymerase molecules that bind to form a filterable polymerase-promoter complex. We show that two holoenzyme molecules interact with the tyrT promoter, probably as a dimer. This interaction is inhibited by ppGpp. By contrast a single holoenzyme monomer suffices for complex formation at the lacUV5 promoter. We propose that In vivo promoter selection by monomeric and dimeric forms of the enzyme could coordinate the synthesis of stable RNA with that of mRNA and could also account in part for the switch in transcriptional selectivity during the stringent response.

MeSH Terms

Base Sequence DNA Restriction Enzymes DNA-Directed RNA Polymerases/metabolism Escherichia coli/enzymology Guanine Nucleotides/pharmacology Guanosine Tetraphosphate/pharmacology Kinetics Operon/drug effects Protein Binding

Chemicals

Guanine Nucleotides Guanosine Tetraphosphate DNA-Directed RNA Polymerases DNA Restriction Enzymes

Authors & Affiliations

3 authors, click to expand affiliations / ORCID

Travers A A

Lamond A I

Mace H A

References (27)

27 references, click to expand

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Article Info

Journal

Nucleic acids research

Abbr.

Nucleic Acids Res

ISSN

0305-1048

DOI

10.1093/nar/10.16.5043

Published

1982-08-25

Pages

5043-57

Language

English

Region

England

NLM ID

0411011

PMCID

PMC320850

Subset

External Links

PubMed source DOI: 10.1093/nar/10.16.5043 PMC Full Text View journal details

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PpGpp regulates the binding of two RNA polymerase molecules to the tyrT promoter.

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