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PMID: 4923072 Published · ppublish English Journal Article

Interaction between histidyl transfer ribonucleic acid and the first enzyme for histidine biosynthesis of Salmonella typhimurium.

Journal of bacteriology ·Vol. 104 ·No. 2 ·1970-11-00 ·Pages 787-92

Kovach JS, Phang JM, Blasi F, Barton RW, Ballesteros-Olmo A, Goldberger RF

Abstract

Previous studies showed that the enzyme (phosphoribosyltransferase) which catalyzes the first step of the histidine pathway in Salmonella typhimurium plays a role in regulation of the histidine operon. Since histidyl transfer ribonucleic acid (His-tRNA) is required for repression of the histidine operon, we considered the possibility that the role of phosphoribosyltransferase might be realized through an interaction with His-tRNA. One prediction inherent in this idea is that the enzyme should interact with His-tRNA in vitro. Evidence is presented for such an interaction. Binding of (3)H-His-tRNA to purified phosphoribosyltransferase was tested on Sephadex columns and on nitrocellulose filters. The enzyme was found to have a high affinity for tRNA. Comparing the binding of (3)H-His-tRNA with that of tRNA aminoacylated with other (3)H-amino acids disclosed that the binding of the histidyl species of tRNA is favored over that of other species and is dependent upon magnesium-ion concentration.

MeSH Terms
Acrylates Amino Acids/metabolism Carbon Isotopes Chromatography Electrophoresis Filtration Gels Histidine/biosynthesis In Vitro Techniques Magnesium/pharmacology Nucleotides/metabolism Protein Binding RNA, Transfer/isolation & purification Salmonella typhimurium/enzymology,metabolism Transferases/isolation & purification Tritium
Chemicals
Acrylates Amino Acids Carbon Isotopes Gels Nucleotides Tritium Histidine RNA, Transfer Transferases Magnesium
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Kovach J S
Phang J M
Blasi F
Barton R W
Ballesteros-Olmo A
Goldberger R F
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22 references, click to expand
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
Published
1970-11-00
Pages
787-92
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC285059
Subset
IM
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