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Journal of Bacteriology, January 1999, p. 648-655, Vol. 181, No. 2
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

NAD-Dependent DNA-Binding Activity of the Bifunctional NadR Regulator of Salmonella typhimurium

Thomas Penfounddagger and John W. Foster*

Department of Microbiology and Immunology, College of Medicine, University of South Alabama, Mobile, Alabama 36688

Received 27 August 1998/Accepted 10 November 1998

NadR is a 45-kDa bifunctional regulator protein. In vivo genetic studies indicate that NadR represses three genes involved in the biosynthesis of NAD. It also participates with an integral membrane protein (PnuC) in the import of nicotinamide mononucleotide, an NAD precursor. NadR was overexpressed and purified as a His-tagged fusion in order to study its DNA-binding properties. The protein bound to DNA fragments containing NAD box consensus sequences. NAD proved to be the relevant in vivo corepressor, but full NAD dependence of repressor activity required nucleotide triphosphates. DNA footprint analysis and gel shift assays suggest that NadR binds as a multimer to adjacent NAD boxes. The DNA-repressor complex would sequester a potential RNA polymerase binding site and thereby decrease expression of the nad regulon.

* Corresponding author. Mailing address: Department of Microbiology and Immunology, College of Medicine, University of South Alabama, Mobile, AL 36688. Phone: (334) 460-6323. Fax: (334) 460-7931. E-mail: fosterj{at}sungcg.usouthal.edu.

dagger Present address: St. Jude Children's Research Hospital, Department of Infectious Diseases, 332 North Lauderdale St., Memphis, TN 38105.

Journal of Bacteriology, January 1999, p. 648-655, Vol. 181, No. 2
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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