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PMID: 1052526 Published · ppublish English Journal Article

Specific binding of the first enzyme for histidine biosynthesis to the DNA of histidine operon.

Nucleic acids research ·Vol. 2 ·No. 11 ·1975-11-00 ·Pages 2021-36

Meyers M, Blasi F, Bruni CB, Deeley RG, Kovach JS, Levinthal M, Mullinix KP, Vogel T, Goldberger RF

Abstract

Studies were done to examine direct binding of the first enzyme of the histidine biosynthetic pathway (phosphoribosyltransferase) to 32P-labeled phi80dhis DNA and competition of this binding by unlabeled homologous DNA and by various preparations of unlabeled heterologous DNA, including that from a defective phi80 bacteriophage carrying the histidine operon with a deletion of part of its operator region. Our findings show that phosphoribosyltransferase binds specifically to site in or near the regulatory region of the histidine operon. The stability of the complex formed by interaction of the enzyme with the DNA was markedly decreased by the substrates of the enzyme and was slightly increased by the allosteric inhibitor, histidine. These findings are consistent with previous data that indicate that phosphoribosyltransferase plays a role in regulating expression of the histidine operon.

MeSH Terms
ATP Phosphoribosyltransferase/genetics,metabolism Adenosine Triphosphate/pharmacology DNA, Bacterial/genetics,metabolism Histidine/biosynthesis,genetics,pharmacology Operon Pentosyltransferases/genetics Phosphoribosyl Pyrophosphate/pharmacology Protein Binding Salmonella Phages/genetics
Chemicals
DNA, Bacterial Histidine Phosphoribosyl Pyrophosphate Adenosine Triphosphate Pentosyltransferases ATP Phosphoribosyltransferase
Authors & Affiliations
9 authors, click to expand affiliations / ORCID
Meyers M
Blasi F
Bruni C B
Deeley R G
Kovach J S
Levinthal M
Mullinix K P
Vogel T
Goldberger R F
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Article Info
Journal
Nucleic acids research
Abbr.
Nucleic Acids Res
ISSN
0305-1048
DOI
10.1093/nar/2.11.2021
Published
1975-11-00
Pages
2021-36
Language
English
Region
England
NLM ID
0411011
PMCID
PMC343569
Subset
IM
External Links
PubMed source DOI: 10.1093/nar/2.11.2021 PMC Full Text View journal details
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