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Nicotinamide mononucleotide adenylyltransferase uses its NAD+ substrate-binding site to chaperone phosphorylated Tau

• Authors : Ma, Xiaojuan; Zhu, Yi; Lu, Jinxia ...

• Source: eLife ; volume 9 ; ISSN 2050-084X

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Semisynthetic biosensors for mapping cellular concentrations of nicotinamide adenine dinucleotides

• Authors : Sallin, Olivier; Reymond, Luc; Gondrand, Corentin ...

• Source: eLife ; volume 7 ; ISSN 2050-084X

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Nicotinamide adenine dinucleotide is transported into mammalian mitochondria

• Authors : Davila, Antonio; Liu, Ling; Chellappa, Karthikeyani ...

• Source: eLife ; volume 7 ; ISSN 2050-084X

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Pharmacological augmentation of nicotinamide phosphoribosyltransferase (NAMPT) protects against paclitaxel-induced peripheral neuropathy

• Authors : LoCoco, Peter M; Risinger, April L; Smith, Hudson R ...

• Source: eLife ; volume 6 ; ISSN 2050-084X

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A lectin receptor kinase as a potential sensor for extracellular nicotinamide adenine dinucleotide in Arabidopsis thaliana

• Authors : Wang, Chenggang; Zhou, Mingqi; Zhang, Xudong ...

• Source: eLife ; volume 6 ; ISSN 2050-084X

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Figure 6—figure supplement 2. Nicotinic acid variations in response to external adenine availability are abolished in npt1 and kcs1 mutants fed with nicotinamide. ; Wild-type (BY4742) and knock-out mutant strains (npt1: Y5581 and kcs1: Y2337) were exponentially grown for 24 hr in SDcasaWU-NA medium (lacking nicotinic acid), supplemented with nicotinamide, as an external pyridine source, and containing (red dots) or not (blue dots) adenine. Quantifications were determined from independent metabolite extractions (N ≥ 3) and standard deviation is presented. The amount measured in wild-type cells grown in the presence of adenine was set at one and indicated p-values were calculated from a Welch’s t-test.

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Figure 6. NNMT gene expression is induced during osteogenic differentiation and affects ZBTB16 and ALPL expression. ; (A–B) NNMT expression during osteogenic differentiation as analyzed by RT-QPCR and western blot. RT-QPCR data represents mean ± SD from three biological replicates. *p = 0.0223, **p = 0.0011, ****p < 0.0001, significance was calculated by two-way ANOVA using Bonferroni's multiple comparisons test. (C) Schematic presentation of the biochemical reaction whereby NNMT transfers a methyl group from SAM (S-adenosyl methionine) to nicotinamide, producing 1MNA (one methyl nicotinamide) and SAH (S-adenosyl homocysteine). (D) SAM levels measured by a fluorescence based assay (Mediomics) in hMSCs before and after osteogenic differentiation for 2 days. The data shown are averages of three biological replicates (p value = 0.01, two tailed t-test). (E) NNMT knockdown using siRNA in naive and osteogenic differentiated hMSCs, assessed by RT-QPCR. Two different siRNAs were used for knockdown of NNMT expression. Experiments shown are mean ± SD from three biological replicates. (F) Expression of ZBTB16 after NNMT knockdown analyzed by RT-QPCR. Experiments shown are mean ± SD from two biological replicates. (G) Expression of ALPL after NNMT knockdown analyzed by RT-QPCR. Experiments shown are mean ± SD from two biological replicates. ****p < 0.0001, statistical significance was calculated by two-way ANOVA using Tukey’s multiple comparisons test.

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Figure 1. Working model for the regulation of NAD homeostasis by NrtR in Mycobacterium. ; (A) The genetic context of nrtR and its signature in Mycobacterium compared with the NrtR-binding sequences in Streptococcus (B) and Mycobacterium (C). (D) NrtR acts as an auto-repressor and represses the transcription of the nadA-nadB-nadC operon that is responsible for the de novo synthesis of the NAD+ cofactor in Mycobacterium. (E) NAD+ homeostasis proceeds through cooperation of a salvage pathway with de novo synthesis in Mycobacterium. Designations: nadA, the gene encoding quinolinate synthase; nadB, gene encoding L-aspartate oxidase; nadC, gene encoding quinolinate phosphoribosyltransferase; PncA, nicotinamide deaminase; PncB, nicotinate phosphoribosyltransferase; NrtR, a bifunctional transcriptional factor involved in the regulation of NAD+ synthesis; ADP-R, ADP-ribose; Na, nicotinic acid; Nm, nicotinamide; Rib-P, ribose-5-phosphate; Asp, aspartate; NaMN, nicotinate mononucleotide; NAD+, nicotinamide adenine dinucleotide; CobB, an NAD+-consuming deacetylase.

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Figure 2—figure supplement 1. Separation of intracellular metabolites by high-performance ion chromatography. ; A prototrophic yeast strain (FY4) was grown in SDcasaWU medium ±Adenine. Metabolite extraction and separation by liquid chromatography were performed as described in the Materials and methods section. (A) Typical entire chromatograms obtained at 260 nm in the presence (red line) or the absence (blue line) of external adenine (Ade). Similar patterns were found in all metabolic extractions presented in Figure 2. Identified peaks are indicated with a color code corresponding to metabolite families. (B) Zooms of absorbance signals obtained from chromatogram at indicated wavelengths. ADP: adenosine 5’-diphosphate, AMP: adenosine 5’-monophosphate, ATP: adenosine 5’-triphosphate, CDP: cytidine 5’-diphosphate, CMP: cytidine 5’-monophosphate, CTP: cytidine 5’-triphosphate, GDP: guanosine 5’-diphosphate, GTP: guanosine 5’-triphosphate, NAD+: nicotinamide adenine dinucleotide, NADH: nicotinamide adenine dinucleotide reduced form, NADPH: phosphorylated form of NADH, SAICAR: succinyl-aminoimidazole carboxamide ribonucleoside, UDP: uridine 5’-diphosphate, UDP-NAG: uridine 5’-diphosphate-N-acetyl glucosamine, UTP: uridine 5’-triphosphate, ZMP: 5-amino-4-imidazole carboxamide ribonucleotide 5′-phosphate and SZMP: succinyl-ZMP.

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Author response: Nicotinamide mononucleotide adenylyltransferase uses its NAD+ substrate-binding site to chaperone phosphorylated Tau

• Authors : Ma, Xiaojuan; Zhu, Yi; Lu, Jinxia

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