Incorporation of histidine into the pyrimidine moiety of thiamin in Saccharomyces cerevisiae

Tazuya, Keiko; Yamada, Kazuko; Kumaoka, Hiroshi

doi:10.1016/s0304-4165(89)80014-5

Cited by 34 publications

(28 citation statements)

References 7 publications

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“…In some organisms such as yeast, the synthesis of the HMP moiety does not involve an intermediate metabolite in purine biosynthesis and depends on histidine as an HMP precursor (Tazuya et al 1989(Tazuya et al , 1993Maundrell 1990;Ishida et al 2008). However, to our knowledge, this is the first demonstration that the early purine enzymes can be bypassed for thiamine synthesis in bacteria.…”

Section: Discussionmentioning

confidence: 89%

Plasticity in the Purine–Thiamine Metabolic Network of Salmonella

Bazurto

Downs

2011

Genetics

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In Salmonella enterica, 5-aminoimidazole ribonucleotide (AIR) is the precursor of the 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP) pyrophosphate moiety of thiamine and the last intermediate in the common HMP/purine biosynthetic pathway. AIR is synthesized de novo via five reactions catalyzed by the purF, -D, -T, -G, and -I gene products. In vivo genetic analysis demonstrated that in the absence of these gene products AIR can be generated if (i) methionine and lysine are in the growth medium, (ii) PurC is functional, and (iii) 5-amino-4-imidazolecarboxamide ribotide (AICAR) has accumulated. This study provides evidence that the five steps of the common HMP/purine biosynthetic pathway can be bypassed in the synthesis of AIR and thus demonstrates that thiamine synthesis can be uncoupled from the early purine biosynthetic pathway in bacteria.

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Section: Discussionmentioning

confidence: 89%

Plasticity in the Purine–Thiamine Metabolic Network of Salmonella

Bazurto

Downs

2011

Genetics

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“…After each tracer had been added to the medium, the labelled atoms of amino acids in cell protein were calculated. The incorporation rate of the label of [2][3][4][5][6][7][8][9][10][11][12][13] C]-glycine was 37.0% into the thiazole, 33.0% into glycine in protein, and 1.27% into tyrosine in protein. The incorporation rates of thiazole and glycine in protein were therefore very similar.…”

Section: Resultsmentioning

confidence: 99%

“…The pyrimidine is formed by ring expansion of imidazole with the insertion of the C-4′, C-5′ fragment of the ribose residue of AIR (10,11). In eukaryotes, we have shown that the N-3, C-4 and amino-N atoms of the pyrimidine are derived from the N-1, C-2 and N-3 atoms of the imidazole ring of histidine as a unit (12,13), while a unit consisting of C-2′, C-2, N-1, C-6, C-5 and C-5′ from pyridoxine is incorporated into the same location in the pyrimidine (14,15).…”

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confidence: 99%

The Biosynthesis of the Thiazole Moiety of Thiamin in the Archaeon <i>Halobacterium salinarum</i>

Hayashi

Kijima

Tazuya-Murayama

et al. 2015

J Nutr Sci Vitaminol

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SummaryThe biosynthetic pathways of the thiazole moiety of thiamin were studied in the archaeon Halobacterium salinarum. Thiamin is generated by the union of 4-amino-5-hydroxymethyl-2-methylpyrimidine (pyrimidine) and 5-(2-hydroxyethyl)-4-methylthiazole (thiazole). The biosynthesis of thiazole is different in facultative anaerobes, aerobes and eukaryotes. In eukaryotes, the C-4, -4′, -5, -5′ and -5″ of the thiazole is biosynthesized from nicotinamide adenine dinucleotide (NAD), with cysteine as S donor and the C-2 and N atoms of glycine. In facultative anaerobic bacteria, such as Escherichia coli, the precursors of the thiazole are the N and C-2 atoms from tyrosine and C-4, -4′, -5, -5′ and -5″ from 1-deoxy-dxylurose-5-phosphate, again with cysteine as S donor. In aerobic bacteria, such as Bacillus subtilis, l-tyrosine is replaced by glycine. In Archaea, known as the third domain of life, the biosynthetic pathway of thiamin has not yet been elucidated. In the present study in the archaeon H. salinarum, it was shown that both the N and C-2 from glycine are incorporated into the thiazole, rather than the N atom coming from l-tyrosine. These results show that thiazole biosynthesis in H. salinarum more closely resembles the biosynthetic pathway found in eukaryotes.

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“…Thiamin is formed by the condensation of its phosphorylated precursors hydroxyethylthiazole phosphate and HMP-PP. HMP-PP is itself derived from pyridoxine (vitamin B 6 ) (Tazuya et al, 1993). There has been a report of an alternative but unrelated HMP biosynthetic pathway that functions when S. cerevisiae is grown under anaerobic conditions (Tanaka et al, 2000).…”

Section: Introductionmentioning

confidence: 99%

The THI5 gene family of Saccharomyces cerevisiae: distribution of homologues among the hemiascomycetes and functional redundancy in the aerobic biosynthesis of thiamin from pyridoxine

Wightman

Meacock

2003

Microbiology

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The THI5 gene family of Saccharomyces cerevisiae comprises four highly conserved members named THI5 (YFL058w), THI11 (YJR156c), THI12 (YNL332w) and THI13 (YDL244w). Each gene copy is located within the subtelomeric region of a different chromosome and all are homologues of the Schizosaccharomyces pombe nmt1 gene which is thought to function in the biosynthesis of hydroxymethylpyrimidine (HMP), a precursor of vitamin B 1 , thiamin. A comprehensive phylogenetic study has shown that the existence of THI5 as a gene family is exclusive to those yeasts of the Saccharomyces sensu stricto subgroup. To determine the function and redundancy of each of the S. cerevisiae homologues, all combinations of the single, double, triple and quadruple deletion mutants were constructed using a PCR-mediated gene-disruption strategy. Phenotypic analyses of these mutant strains have shown the four genes to be functionally redundant in terms of HMP formation for thiamin biosynthesis; each promotes synthesis of HMP from the pyridoxine (vitamin B 6 ) biosynthetic pathway. Furthermore, growth studies with the quadruple mutant strain support a previous proposal of an alternative HMP biosynthetic pathway that operates in yeast under anaerobic growth conditions. Comparative analysis of mRNA levels has revealed subtle differences in the regulation of the four genes, suggesting that they respond differently to nutrient limitation.

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Incorporation of histidine into the pyrimidine moiety of thiamin in Saccharomyces cerevisiae

Cited by 34 publications

References 7 publications

Plasticity in the Purine–Thiamine Metabolic Network of Salmonella

Plasticity in the Purine–Thiamine Metabolic Network of Salmonella

The Biosynthesis of the Thiazole Moiety of Thiamin in the Archaeon <i>Halobacterium salinarum</i>

The THI5 gene family of Saccharomyces cerevisiae: distribution of homologues among the hemiascomycetes and functional redundancy in the aerobic biosynthesis of thiamin from pyridoxine

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