ArticleJournal of bacteriology2005
Coupling of NAD+ biosynthesis and nicotinamide ribosyl transport: characterization of NadR ribonucleotide kinase mutants of Haemophilus influenzae.
Article in Journal of bacteriology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 21 citations in OpenAlex.
- Regulation of NADMetabolism: clinical and experimental · 2022Review
- Nicotinamide mononucleotide production by fructophilic lactic acid bacteria.Scientific reports · 2021Article
- Structural and Functional Characterization of NadR fromMolecules (Basel, Switzerland) · 2020Article
- Meat Intake and the Dose of Vitamin BInternational journal of tryptophan research : IJTR · 2017Review
- Crystal structure of the vitamin B3 transporter PnuC, a full-length SWEET homolog.Nature structural & molecular biology · 2014Article
- Characterization of lactate utilization and its implication on the physiology of Haemophilus influenzae.International journal of medical microbiology : IJMM · 2014Article
- The transporter-opsin-G protein-coupled receptor (TOG) superfamily.The FEBS journal · 2013Article
- Evolution of the oligopeptide transporter family.The Journal of membrane biology · 2011Article
- Regulation of yeast sirtuins by NAD(+) metabolism and calorie restriction.Biochimica et biophysica acta · 2010Review
- Article
- Biosynthesis and recycling of nicotinamide cofactors in mycobacterium tuberculosis. An essential role for NAD in nonreplicating bacilli.The Journal of biological chemistry · 2008Article
- NAD+ utilization in Pasteurellaceae: simplification of a complex pathway.Journal of bacteriology · 2006Review
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Authors and funding
3 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Previously, we characterized a pathway necessary for the processing of NAD+ and for uptake of nicotinamide riboside (NR) in Haemophilus influenzae. Here we report on the role of NadR, which is essential for NAD+ utilization in this organism. Different NadR variants with a deleted ribonucleotide kinase domain or with a single amino acid change were characterized in vitro and in vivo with respect to cell viability, ribonucleotide kinase activity, and NR transport. The ribonucleotide kinase mutants were viable only in a nadV+ (nicotinamide phosphoribosyltransferase) background, indicating that the ribonucleotide kinase domain is essential for cell viability in H. influenzae. Mutations located in the Walker A and B motifs and the LID region resulted in deficiencies in both NR phosphorylation and NR uptake. The ribonucleotide kinase function of NadR was found to be feedback controlled by NAD+ under in vitro conditions and by NAD+ utilization in vivo. Taken together, our data demonstrate that the NR phosphorylation step is essential for both NR uptake across the inner membrane and NAD+ synthesis and is also involved in controlling the NAD+ biosynthesis rate.
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