A comparative study of the regulation of nicotinamide-adenine dinucleotide biosynthesis

Saxton, Romaine E.; Rocha, Victor; Rösser, Ralf; Andreoli, Anthony J.; Shimoyama, Makoto; Kosaka, Atsuko; Chandler, Jerry L. R.; Gholson, R.K.

doi:10.1016/0304-4165(68)90106-2

Cited by 30 publications

(23 citation statements)

References 26 publications

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“…1)' but this possibility was not investigated because expression of the nadC gene is unaffected by exogenous nicotinate (Saxton et al, 1968). Also, where tested, expression of the ace operon in Nad-deletion mutants (Ace+ and 'Ace-') was still subject to normal regulatory stimuli.…”

Section: Discussionmentioning

confidence: 99%

Biochemical Genetics of the -Keto Acid Dehydrogenase Complexes of Escherichia coli K 12: Genetic Characterization and Regulatory Properties of Deletion Mutants

Langley

Guest

1978

Journal of General Microbiology

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103Twenty-eight spontaneous auxotrophic aroP mutants with deletions in the azi-nadC-aroPaceE-aceF-lpd region of the Esclwricliia coli ~1 2 chromosome were characterized genetically with respect to various azi, nadC, ace and Ipd markers by PI-mediated transduction. One mutant (~A 1 8 ;aroP-lpd-') had a deletion which extended through the aceE and aceF genes to end within the Ipd gene. The polarity of the ace operon (aceE to aceF) was confirmed. It was concluded that 10 out of 15 deletions generating a strict requirement for acetate terminated in the aceE gene. Of the ten, three mutants (~A 2 2 , cA41 and cA42) synthesized detectable dihydrolipoamide acetyltransferase (the aceF gene product) and seven were assumed to possess deletions generating polar effects on aceF gene expression. Five deletions appeared to extend into the aceF gene. A further five deletions, which limited the expression of the ace operon without generating an Ace-phenotype or a complete Ace-phenotype, ended closest to the aroP-proximal aceE markers. The opposite ends of all these deletions appeared to terminate before (lo), within (2) or extend beyond (9) the nadC gene. There was no obvious correlation between the deletion end-points and the corresponding lipoamide dehydrogenase activities, which ranged from 30 to 95 of parental levels in different deletion strains. The remaining seven deletions simply extended between the aroP and nadC genes (nad-aroPA) without affecting expression of the ace operon.Regulation of the synthesis of the pyruvate and a-ketoglutarate dehydrogenase complexes was investigated in some of the parental and deletion strains under different physiological conditions including thiamin-deprivation. The results indicate that the syntheses of the two dehydrogenase complexes are independently regulated. Expression of the Zpd gene appears to be coupled to complex synthesis but can be dissociated under some conditions. Mechanisms for regulating Ipd gene expression are discussed and an autogenous mechanism involving uncomplexed lipoamide dehydrogenase functioning as a negatively acting repressor at the operator site of an independent Ipd gene is proposed as the simplest mechanism which is consistent with all available information. I N T R O D U C T I O NMutants of Eschericl7ia coli ~1 2 requiring acetate for aerobic growth on glucose and lacking overall pyruvate dehydrogenase complex (pdh complex) activity have been characterized as: aceE mutants, lacking activity of the dehydrogenase (Elp) component; aceF mutants, lacking dihydrolipoamide acetyltransferase (E2p) activity; and polar aceE mutants (mainly of the nonsense type), lacking both E l p and E2p activities (Henning et aZ., 1966(Henning et aZ., , 1968(Henning et aZ., , 1969. The mutations are clustered at approximately 2 min in the E. coli linkage map and those of the third class are confined to a relatively large segment at one * Present address : Beecham Pharmaceuticals, Clarendon Road, Worthing, West Sussex, BN14 8QH.

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Section: Discussionmentioning

confidence: 99%

Biochemical Genetics of the -Keto Acid Dehydrogenase Complexes of Escherichia coli K 12: Genetic Characterization and Regulatory Properties of Deletion Mutants

Langley

Guest

1978

Journal of General Microbiology

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“…The NAD biosynthetic pathway in Bacillus subtilis has been thought to be the same as in E. coli (7), although the regulation of some of the B. subtilis enzymes, for example, Qa phosphoribosyltransferase, may be rather different than in E. coli (28). Nic-requiring auxotrophic mutants have been isolated in B. subtilis, and the mutations (termed nic) were mapped near the spoOB-pheBA region (2,10,13).…”

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confidence: 99%

Cloning, nucleotide sequence, and regulation of the Bacillus subtilis nadB gene and a nifS-like gene, both of which are essential for NAD biosynthesis

Sun

Setlow

1993

J Bacteriol

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NAD plays an important role in cellular metabolism, as it functions as a cofactor in numerous oxidation-reduction reactions. NAD is synthesized from quinolinic acid (Qa) via a pathway which is similar in all organisms which have been examined (Fig. 1). On the other hand, the pathway for Qa formation differs in different organisms (7). In Escherichia coli and Salmonella typhimurium, as well as in many other eubacteria, Qa is synthesized from L-aspartate and dihydroxyacetone phosphate by a Qa synthetase complex (7,33). This complex consists of two enzymes, L-aspartate oxidase and Qa synthetase A. Aspartate oxidase catalyzes oxidation of L-aspartate to iminoaspartate, which is subsequently condensed with dihydroxyacetone phosphate by Qa synthetase A to form Qa (Fig. 1). In E. coli, the latter two enzymes are encoded by the unlinked genes nadB and nadA4, respectively, both of which have been cloned and sequenced (6). Qa is then converted to nicotinic acid mononucleotide (NaMN) by Qa phosphoribosyltransferase, which is coded for by the nadC gene (23). NaMN then reacts with ATP in a reaction catalyzed by the nadD gene product to give nicotinic acid adenine dinucleotide, which is then amidated by the nadE gene product to form NAD. Cells can also convert exogenous nicotinic acid (Nic) to NaMN by Nic phosphoribosyltransferase. When either nadA, nadB, or nadC is inactivated, cells become dependent on Nic for growth.The NAD biosynthetic pathway in Bacillus subtilis has been thought to be the same as in E. coli (7), although the regulation of some of the B. subtilis enzymes, for example, Qa phosphoribosyltransferase, may be rather different than in E. coli (28). Nic-requiring auxotrophic mutants have been isolated in B. subtilis, and the mutations (termed nic) were mapped near the spoOB-pheBA region (2,10,13 The chromosomal DNA library was used to transform strain PS1589 to chloramphenicol resistance. Strain PS1589 carries the divIVB1 mutation, which is known to be closely linked to the site of nic mutations (16,26). Several different Cmr transformants were found to have the cat gene closely linked to divIVB1. Three-factor crosses showed that in one of the Cmr transformants, strain PS1591, the order of markers was divIVB-spoOB-cat.

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“…The nadC gene maps to 3 min on the Salmonella chromosome, and together with the unlinked nadA and nadB genes, it is one of three nonessential genes involved in the de novo biosynthesis of NAD and NADP (28). Both nadA and nadB are regulated by the nadI (or nadR) repressor (6,8,12,38), while nadC is not known to be under any genetic regulation (11,31).…”

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The Salmonella typhimurium nadC gene: sequence determination by use of Mud-P22 and purification of quinolinate phosphoribosyltransferase

et al. 1993

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A comparative study of the regulation of nicotinamide-adenine dinucleotide biosynthesis

Cited by 30 publications

References 26 publications

Biochemical Genetics of the -Keto Acid Dehydrogenase Complexes of Escherichia coli K 12: Genetic Characterization and Regulatory Properties of Deletion Mutants

Biochemical Genetics of the -Keto Acid Dehydrogenase Complexes of Escherichia coli K 12: Genetic Characterization and Regulatory Properties of Deletion Mutants

Cloning, nucleotide sequence, and regulation of the Bacillus subtilis nadB gene and a nifS-like gene, both of which are essential for NAD biosynthesis

The Salmonella typhimurium nadC gene: sequence determination by use of Mud-P22 and purification of quinolinate phosphoribosyltransferase

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