Isolating the Arabidopsis thaliana Genes for de Novo Purine Synthesis by Suppression of Escherichia coli Mutants (I. 5[prime]-Phosphoribosyl-5-Aminoimidazole Synthetase)

Senecoff, Julie F.; Meagher, Richard B.

doi:10.1104/pp.102.2.387

Cited by 38 publications

(29 citation statements)

References 31 publications

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“…ATTTTTGTTT(A)67 ( Senecoff and Meagher, 1993). The genomic clone contains a putative transit peptide of 58 amino acids with exact identity to the 40 amino acid of the deduced amino acid translation of our cDNA clone.…”

Section: Discussionmentioning

confidence: 99%

“…Concerning compartmentalization of these three enzymes, evidence for a plastidic transit peptide sequence has already been presented for Arabidopsis AIR synthetase by Senecoff and Meagher (1993). Their conclusions were based on comparison of the N-terminal sequence of Arabidopsis AIR synthetase with concensus rules for chloroplast transit peptides (Gavel and von Heijne, 1990;von Heijne and Nishikawa,1991 ;von Heijne et a/., 1989).…”

Section: Discussionmentioning

confidence: 99%

“…Recently, a cDNA from Arabidopsis thaliana encoding AIR synthetase, the enzyme catalysing the fifth step of the purine biosynthetic pathway, has been cloned and its nucleotide sequence determined (Senecoff and Meagher, 1993). Based on analysis of the coding region of the cDNA, the authors suggested a one gene, one enzyme (purD, purN, purM) are circled.…”

Section: Introductionmentioning

confidence: 99%

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Molecular characterization of Arabidopsis thaliana cDNAs encoding three purine biosynthetic enzymes

Schnorr¹,

Nygaard

Laloue³

1994

The Plant Journal

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Molecular characterization of Arabidopsis thaliana cDNAs encoding three purine biosynthetic enzymes

Schnorr¹,

Nygaard

Laloue³

1994

The Plant Journal

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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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“…The cDNA sequences of all the plant purine biosynthetic (pur) genes studied have 5Ј extensions relative to the coding regions of the corresponding Escherichia coli genes (Senecoff and Meagher, 1993;Chapman et al, 1994;Schnorr et al, 1994Schnorr et al, , 1996Kim et al, 1995;Senecoff et al, 1996;Smith et al, 1998). These extensions potentially encode N-terminal, organelle-targeting sequences and indicate that in contrast to other eukaryotes (Gooljarsingh et al, 2001), the pathway is likely to be organelle-localized in plants.…”

mentioning

confidence: 99%

Dual Intracellular Localization and Targeting of Aminoimidazole Ribonucleotide Synthetase in Cowpea

Goggin¹,

Lipscombe²,

Fedorova³

et al. 2003

Plant Physiology

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De novo purine biosynthesis is localized to both mitochondria and plastids isolated from Bradyrhizobium sp.-infected cells of cowpea (Vigna unguiculata L. Walp) nodules, but several of the pathway enzymes, including aminoimidazole ribonucleotide synthetase (AIRS [EC 6.3.3.1], encoded by Vupur5), are encoded by single genes. Immunolocalization confirmed the presence of AIRS protein in both organelles. Enzymatically active AIRS was purified separately from nodule mitochondria and plastids. N-terminal sequencing showed that these two isoforms matched the Vupur5 cDNA sequence but were processed at different sites following import; the mitochondrial isoform was five amino acids longer than the plastid isoform. Electrospray tandem mass spectrometry of a trypsin digest of mitochondrial AIRS identified two internal peptides identical with the amino acid sequence deduced from Vupur5 cDNA. Western blots of proteins from mitochondria and plastids isolated from root tips showed a single AIRS protein present at low levels in both organelles. 35 S-AIRS protein translated from a Vupur5 cDNA was imported into isolated pea (Pisum sativum) leaf chloroplasts in vitro by an ATPdependent process but not into import-competent mitochondria from several plant and non-plant sources. Components of the mature protein are likely to be important for import because the N-terminal targeting sequence was unable to target green fluorescent protein to either chloroplasts or mitochondria in Arabidopsis leaves. The data confirm localization of the protein translated from the AIRS gene in cowpea to both plastids and mitochondria and that it is cotargeted to both organelles, but the mechanism underlying import into mitochondria has features that are yet to be identified.In root nodules of legumes of the tribe Phaseoleae, symbiotically fixed N 2 is assimilated by de novo purine biosynthesis, after which the purines are oxidized to allantoin and allantoic acid (Atkins and Smith, 2000). It is in this form that fixed N is exported in xylem from the nodule to the shoot. The 10 enzymes of the purine biosynthetic pathway have been well studied in relation to their role in cancer metabolism, and the genes encoding them cloned from a wide variety of organisms. However, in plants, far less is known about the enzymes of the pathway, although genes encoding a number have now been isolated (Atkins and Smith, 2000).The cDNA sequences of all the plant purine biosynthetic (pur) genes studied have 5Ј extensions relative to the coding regions of the corresponding Escherichia coli genes (Senecoff and Meagher, 1993;Chapman et al., 1994;Schnorr et al., 1994Schnorr et al., , 1996Kim et al., 1995;Senecoff et al., 1996;Smith et al., 1998). These extensions potentially encode N-terminal, organelle-targeting sequences and indicate that in contrast to other eukaryotes (Gooljarsingh et al., 2001), the pathway is likely to be organelle-localized in plants. This was confirmed in a recent study that showed that in cowpea (Vigna unguiculata L. Walp) nodules, both the mitochondria ...

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Isolating the Arabidopsis thaliana Genes for de Novo Purine Synthesis by Suppression of Escherichia coli Mutants (I. 5[prime]-Phosphoribosyl-5-Aminoimidazole Synthetase)

Cited by 38 publications

References 31 publications

Molecular characterization of Arabidopsis thaliana cDNAs encoding three purine biosynthetic enzymes

Molecular characterization of Arabidopsis thaliana cDNAs encoding three purine biosynthetic enzymes

Identification of sugarcane genes involved in the purine synthesis pathway

Dual Intracellular Localization and Targeting of Aminoimidazole Ribonucleotide Synthetase in Cowpea

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