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. 1974 Jul;1(7):881–888. doi: 10.1093/nar/1.7.881

Defective in vitro binding of histidyl-transfer ribonucleic acid to feedback resistant phosphoribosyl transferase of Salmonella typhimurium

Oliver Smith 1, Marilyn M Meyers 1, Tikvah Vogel 1, Roger D Deeley 1, Robert Goldberger 1
PMCID: PMC343391  PMID: 10793720

Abstract

We previously proposed that the first enzyme for histidine biosynthesis in Salmonellatyphimurium plays a role in regulating expression of the histidine operon and that in order to play this role the enzyme must form a complex with histidyl-tRNA. Among the many observations that led to these conclusions were 1) that regulation of the histidine operon is defective in strains carrying a mutation in the gene for the first enzyme that renders the enzyme resistant to inhibition by histidine; and 2) that the enzyme purified from the wild type strain interacts specifically, and with high affinity, with histidyl-tRNA. The present study was carried out to test the prediction that the enzyme purified from the mutant strain described above would display a defect in its interaction with histidyl-tRNA. This prediction was fulfilled by the finding that purified histidine-insensitive enzyme does not bind histidyl-tRNA. Our results therefore suggest that the capacity of the enzyme to bind histidyl-tRNA invitro is a reflection of its regulatory function invivo.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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