This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Merdanovic, M.
Right arrow Articles by Reidl, J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Merdanovic, M.
Right arrow Articles by Reidl, J.

 Previous Article  |  Next Article 

Journal of Bacteriology, July 2005, p. 4410-4420, Vol. 187, No. 13
0021-9193/05/$08.00+0     doi:10.1128/JB.187.13.4410-4420.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Coupling of NAD+ Biosynthesis and Nicotinamide Ribosyl Transport: Characterization of NadR Ribonucleotide Kinase Mutants of Haemophilus influenzae

Melisa Merdanovic, Elizabeta Sauer, and Joachim Reidl*

Institut für Hygiene und Mikrobiologie, Universität Würzburg, Josef Schneider Str. 2, E1, 97080 Würzburg, Germany

Received 3 February 2005/ Accepted 21 March 2005

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.

* Corresponding author. Mailing address: Institut für Hygiene und Mikrobiologie, Universität Würzburg, Josef Schneider Str. 2, E1, 97080 Würzburg, Germany. Phone: 49 931 20146159. Fax: 49 931 20146445. E-mail: joachim.reidl{at}mail.uni-wuerzburg.de.

Journal of Bacteriology, July 2005, p. 4410-4420, Vol. 187, No. 13
0021-9193/05/$08.00+0     doi:10.1128/JB.187.13.4410-4420.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Boshoff, H. I. M., Xu, X., Tahlan, K., Dowd, C. S., Pethe, K., Camacho, L. R., Park, T.-H., Yun, C.-S., Schnappinger, D., Ehrt, S., Williams, K. J., Barry, C. E. III (2008). Biosynthesis and Recycling of Nicotinamide Cofactors in Mycobacterium tuberculosis: AN ESSENTIAL ROLE FOR NAD IN NONREPLICATING BACILLI. J. Biol. Chem. 283: 19329-19341 [Abstract] [Full Text]  
  • Gerlach, G., Reidl, J. (2006). NAD+ utilization in pasteurellaceae: simplification of a complex pathway.. J. Bacteriol. 188: 6719-6727 [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»