Molecular characterization of <i>Arabidopsis thaliana</i> cDNAs encoding three purine biosynthetic enzymes

Schnorr, Kirk; Nygaard, Per; Laloue, Michel

doi:10.1046/j.1365-313x.1994.6010113.x

Cited by 32 publications

(22 citation statements)

References 15 publications

(24 reference statements)

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“…Each cDNA is reported to code for a product with a single enzymatic domain, a structure similar to prokaryote purine enzymes whereas eukaryote genes typically encode bifunctional (PUR2, PUR5) (Henikoff, 1987) or trifunctional (PUR2, PUR5, PUR3) (Aimi et al, 1990;Henikoff, 1987;Henikoff and Furlong, 1983) enzymes. The prokaryotic, monofunctional enzyme structure predicted by the Arabidopsis PUR2 and PUR3 genes is consistent with the outcome of a phylogenetic comparison of their predicted amino acid sequences with those from other organisms, which shows these to be most similar to the corresponding sequences from bacteria (Schnorr et al, 1994).…”

Section: De Novo Purine Nucleotide Metabolismsupporting

confidence: 73%

“…Using the same functional complementation strategy Schnorr et al (1994) cloned two additional cDNAs encoding purine pathway enzymes: glycineamide ribonucelotide (GAR) synthetase (Genbank accession: X74766; PUR2; EC 6.3.4.13) and GAR formyl transferase (Genbank accession X74767; PUR3; EC 2.1.2.2), respectively. Each cDNA is reported to code for a product with a single enzymatic domain, a structure similar to prokaryote purine enzymes whereas eukaryote genes typically encode bifunctional (PUR2, PUR5) (Henikoff, 1987) or trifunctional (PUR2, PUR5, PUR3) (Aimi et al, 1990;Henikoff, 1987;Henikoff and Furlong, 1983) enzymes.…”

Section: De Novo Purine Nucleotide Metabolismmentioning

confidence: 99%

See 1 more Smart Citation

Purine and Pyrimidine Nucleotide Synthesis and Metabolism

Moffatt

Ashihara

2002

The Arabidopsis Book

266

249

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Section: De Novo Purine Nucleotide Metabolismsupporting

confidence: 73%

Section: De Novo Purine Nucleotide Metabolismmentioning

confidence: 99%

Purine and Pyrimidine Nucleotide Synthesis and Metabolism

Moffatt

Ashihara

2002

The Arabidopsis Book

266

249

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“…PurN homologs have also been characterized in Arabidopsis thaliana and soybean (Glycine max; Schnorr et al, 1994Schnorr et al, , 1996Boldt and Zrenner, 2003). Under aerobic conditions, E. coli can also hydrolyze 10-formyl THF via one of the folate interconversion enzymes, 10-formyl THF deformylase (10-FDF, PurU; EC 3.5.1.10), which releases THF and formate (Nagy et al, 1993).…”

Section: Introductionmentioning

confidence: 99%

Arabidopsis 10-Formyl Tetrahydrofolate Deformylases Are Essential for Photorespiration

et al. 2008

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In prokaryotes, PurU (10-formyl tetrahydrofolate [THF] deformylase) metabolizes 10-formyl THF to formate and THF for purine and Gly biosyntheses. The Arabidopsis thaliana genome contains two putative purU genes, At4g17360 and At5g47435. Knocking out these genes simultaneously results in plants that are smaller and paler than the wild type. These double knockout (dKO) mutant plants show a 70-fold increase in Gly levels and accumulate elevated levels of 5-and 10-formyl THF. Embryo development in dKO mutants arrests between heart and early bent cotyledon stages. Mature seeds are shriveled, accumulate low amounts of lipids, and fail to germinate. However, the dKO mutant is only conditionally lethal and is rescued by growth under nonphotorespiratory conditions. In addition, culturing dKO siliques in the presence of sucrose restores normal embryo development and seed viability, suggesting that the seed and embryo development phenotypes are a result of a maternal effect. Our findings are consistent with the involvement of At4g17360 and At5g47435 proteins in photorespiration, which is to prevent excessive accumulation of 5-formyl THF, a potent inhibitor of the Gly decarboxylase/Ser hydroxymethyltransferase complex. Supporting this role, deletion of the At2g38660 gene that encodes the bifunctional 5,10-methylene THF dehydrogenase/5,10-methenyl THF cyclohydrolase that acts upstream of 5-formyl THF formation restored the wild-type phenotype in dKO plants.

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“…The representative enzyme sequences for each member in the de novo pathway and the corresponding accession numbers are: PRPP synthetase (Arabidopsis thaliana, CAA63552) (Krath et al, 1999), Glutamine-PRPP-amidotransferase (Rattus norvegicus, A46088) (Iwahana et al, 1993), glycinamide ribonucleotide (GAR) synthetase (Arabidopsis thaliana, P52420) (Schnorr, et al, 1994), GAR transformylase (Arabidopsis thaliana, P52422) (Schnorr, et al, 1994), Formylglycinamide ribonucleotide (FGAM) synthetase (Glycine max, AAF21596, unpublished direct submission), 5-aminoimidazole ribonucleotide (AIR) synthetase (Arabidopsis thaliana, Q05728) (Senecoff and Meagher, 1993), AIR carboxylase (Arabidopsis thaliana, T02535, unpublished direct submission), 5-aminoimidazole-4-N-succinocarboxamide ribonucleotide (SAICAR) synthetase (Arabidopsis thaliana, P38025, unpublished direct submission), adenylosuccinate lyase (Leishmania major, CAC22697) (Ivens et al 1998), with AICAR transformylase and IMP cyclohydrolase bifunctional enzymes (Gallus gallus, P31335) (Ni et al, 1991).…”

Section: Methodsmentioning

confidence: 99%

Identification of sugarcane genes involved in the purine synthesis pathway

2001

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Nucleotide synthesis is of central importance to all cells. In most organisms, the purine nucleotides are synthesized de novo from non-nucleotide precursors such as amino acids, ammonia and carbon dioxide. An understanding of the enzymes involved in sugarcane purine synthesis opens the possibility of using these enzymes as targets for chemicals which may be effective in combating phytopathogen. Such an approach has already been applied to several parasites and types of cancer. The strategy described in this paper was applied to identify sugarcane clusters for each step of the de novo purine synthesis pathway. Representative sequences of this pathway were chosen from the National Center for Biotechnology Information (NCBI) database and used to search the translated sugarcane expressed sequence tag (SUCEST) database using the available basic local alignment search tool (BLAST) facility. Retrieved clusters were further tested for the statistical significance of the alignment by an implementation (PRSS3) of the Monte Carlo shuffling algorithm calibrated using known protein sequences of divergent taxa along the phylogenetic tree. The sequences were compared to each other and to the sugarcane clusters selected using BLAST analysis, with the resulting table of p-values indicating the degree of divergence of each enzyme within different taxa and in relation to the sugarcane clusters. The results obtained by this strategy allowed us to identify the sugarcane proteins participating in the purine synthesis pathway.

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Molecular characterization of Arabidopsis thaliana cDNAs encoding three purine biosynthetic enzymes

Cited by 32 publications

References 15 publications

Purine and Pyrimidine Nucleotide Synthesis and Metabolism

Purine and Pyrimidine Nucleotide Synthesis and Metabolism

Arabidopsis 10-Formyl Tetrahydrofolate Deformylases Are Essential for Photorespiration

Identification of sugarcane genes involved in the purine synthesis pathway

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