Activity of the nicotinamide mononucleotide transport system is regulated in Salmonella typhimurium

N. Zhu, B. M. Olivera, J. R. Roth

Research output: Contribution to journalArticle

30 Scopus citations

Abstract

Transport of nicotinamide mononucleotide (NMN) requires two functions, NadI(T) and PnuC. The PnuC protein is membrane associated, as judged by isolation of active TnphoA gene fusions and demonstration that the fusion protein is membrane associated. The PnuC function appears to be the major component of the transport system, since mutant alleles of the pnuC gene permit NMN transport in the absence of NadI(T) function. We present evidence that the activity of the NMN transport system varies in response to internal pyridine levels (presumably NAD). This control mechanism requires NadI(T) function, which is provided by a bifunctiona1 protein encoded by the nadI gene (called nadR by Foster and co-workers [J. W. Foster, Y. K. Park, T. Fenger, and M. P. Spector, J. Bacteriol. 172:4187-4196]). The nadI protein regulates transcription of the nadA and nadB biosynthetic genes and modulates activity of the NMN permease; both regulatory activities respond to the internal pyridine nucleotide level.

Original languageEnglish (US)
Pages (from-to)1311-1320
Number of pages10
JournalJournal of Bacteriology
Volume173
Issue number3
StatePublished - 1991
Externally publishedYes

ASJC Scopus subject areas

  • Applied Microbiology and Biotechnology
  • Immunology

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