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

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.

journal_name

Nucleic Acids Res

journal_title

Nucleic acids research

authors

Smith O,Meyers MM,Vogel T,Deeley RD,Goldberger R

doi

10.1093/nar/1.7.881

keywords:

subject

Has Abstract

pub_date

1974-07-01 00:00:00

pages

881-8

issue

7

eissn

0305-1048

issn

1362-4962

journal_volume

1

pub_type

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