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Nucleic Acids Research, 1975, Vol. 2, No. 11 2021-2036
© 1975

Articles

Specific binding of the first enzyme for histidine biosynthesis to the DNA of the histidine operon

Marilyn Meyers, Francesco Blasi*, Carmelo B. Bruni*, Roger G. Deeley, John S. Kovach**, Mark Levinthal***, Kathleen P. Mullinix, Tikvah Vogel and Robert F. Goldberger

Laboratory of Biochemistry, National Cancer Institute, National Institutes of Health Bethesda, MD 20014, USA

Received July 30, 1975.

Studies were done to examine direct binding of the first enzyme ofthe histidine biosynthetic pathway (phosphoribosyltransferase) to 32Plabeied ø80dhis DNA and competition of this binding by unlabeled homologous DNA and by various preparations of unlabeled heterologous DNA, including that from a defective ø80 bacteriophage carrying the histidine operon with a deletion of part of its operator region. Our findings show that phosphoribosyl transferase binds specifically to a site in or near the regulatory region of the histidine operon. The stability of the complex formed by interaction of the enzyme with the DNA was markedly decreased by the substrates of the enzyme and was slightly increased by the allosteric inhibitor, histidine. These findings are consistent with previous data that indicate that phosphoribosyl transferase plays a rolein regulating expression of the histidine operon.

*Present address: Institute of General Pathology, University of Naples 2nd Medical School, via Sergio Pansini, 1-80131 Naples, Italy

** Present address: Department of Medicine, Columbia University College of Physicians and Surgeons, New York, NY 10032, USA

***Present address: Department of Biological Sciences, Purdue University, Lafayette, IN 47907, USA


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