Interaction Between Histidyl Transfer Ribonucleic Acid and the First Enzyme for Histidine Biosynthesis of Salmonella typhimurium
AUTOR(ES)
Kovach, John S.
RESUMO
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 3H-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 3H-His-tRNA with that of tRNA aminoacylated with other 3H-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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=285059Documentos Relacionados
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