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J Bacteriol. 1971 April; 106(1): 227-237
Copyright © 1971 American Society for Microbiology. All Rights Reserved.

Two Mutations in the First Gene of the Histidine Operon of Salmonella typhimurium Affecting Control

Lucia Rothman-Denes1 and Robert G. Martin

a Laboratory of Molecular Biology, National Institute of Arthritis and Metabolic Diseases, Bethesda, Maryland 20014

ABSTRACT

Two strains with mutations in the first structural gene of the histidine operon of Salmonella typhimurium were characterized. (The first structural gene specifies the first enzyme of histidine biosynthesis, phosphoribosyltransferase, which is sensitive to feedback inhibition by histidine.) One mutation, hisG3934, results in a phosphoribosyltransferase which is no longer sensitive to feedback inhibition by histidine but is instead subject to inhibition by aspartic acid. The other mutation, hisG3935, allows the histidine operon to be partially repressed by several amino acids, including aspartic acid. Analysis of hisG3935 is consistent with the hypothesis that phosphoribosyltransferase is directly involved in the regulation of the histidine operon.


FOOTNOTES

1 Present address: Department of Biophysics, The University of Chicago, Chicago, Ill. 60637.


J Bacteriol. 1971 April; 106(1): 227-237
Copyright © 1971 American Society for Microbiology. All Rights Reserved.




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