Molecular Cloning of the Gene Encoding the L-Asparaginase Gene of Arabidopsis thaliana

Casado, A.; Caballero, José L.; Franco, A. R.; Cárdenas, Jacobo; Grant, Murray; Muñoz‐Blanco, Juan

doi:10.1104/pp.108.3.1321

Cited by 11 publications

(6 citation statements)

References 4 publications

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“…This enzyme was not further characterized, and in any case it represented only a very small fraction of total ASNase activity. The pI value of 4.5 -5.0 inferred from the isoelectric focusing experiment for ASNase is close to the value of 5.2 calculated from the cloned gene of Arabidopsis thaliana by Casado et al (1995) and the value of 4.5 for K + -independent ASNase from L. arboreus (Lough et al, 1992a). Attempts to obtain the N-terminal sequence of the purified protein were unsuccessful, suggesting a possible blocked N-terminal.…”

Section: Discussionsupporting

confidence: 79%

Purification and properties of asparaginase from the testa of immature seeds of pea (Pisum sativum L.)

Chagas

Sodek

2001

Braz. arch. biol. technol.

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Section: Discussionsupporting

confidence: 79%

Purification and properties of asparaginase from the testa of immature seeds of pea (Pisum sativum L.)

Chagas

Sodek

2001

Braz. arch. biol. technol.

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“…A BLAST search of the TAIR database using the predicted amino acid sequence of Arabidopsis L-asparaginase At5g08100 (Casado et al 1995;Hejazi et al 2002), related to the K + -independent L-asparaginases from Lupinus species, retrieved three related sequences from Arabidopsis. The most closely related, At3g16150 (55% sequence identity) was annotated as a putative L-asparaginase.…”

Section: Resultsmentioning

confidence: 99%

“…Using L. arboreus asparaginase cDNA as a probe, genomic and cDNA clones were also isolated for its Arabidopsis homolog, At5g08100 [Arabidopsis genome initiative (AGI) locus number] (Casado et al 1995). Recombinant At5g08100 has the structural hallmarks of Ntn hydrolase superfamily members (Hejazi et al 2002).…”

Section: Introductionmentioning

confidence: 99%

Co-occurrence of both l-asparaginase subtypes in Arabidopsis: At3g16150 encodes a K+-dependent l-asparaginase

Bruneau

Chapman

Marsolais

2006

Planta

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L-asparaginases (EC 3.5.1.1) are hypothesized to play an important role in nitrogen supply to sink tissues, especially in legume-developing seeds. Two plant L-asparaginase subtypes were previously identified according to their K(+)-dependence for catalytic activity. An L-asparaginase homologous to Lupinus K(+)-independent enzymes with activity towards beta-aspartyl dipeptides, At5g08100, has been previously characterized as a member of the N-terminal nucleophile amidohydrolase superfamily in Arabidopsis. In this study, a K(+)-dependent L-asparaginase from Arabidopsis, At3g16150, is characterized. The recombinants At3g16150 and At5g08100 share a similar subunit structure and conserved autoproteolytic pentapeptide cleavage site, commencing with the catalytic Thr nucleophile, as determined by ESI-MS. The catalytic activity of At3g16150 was enhanced approximately tenfold in the presence of K(+). At3g16150 was strictly specific for L-Asn, and had no activity towards beta-aspartyl dipeptides. At3g16150 also had an approximately 80-fold higher catalytic efficiency with L-Asn relative to At5g08100. Among the beta-aspartyl dipeptides tested, At5g08100 had a preference for beta-aspartyl-His, with catalytic efficiency comparable to that with L-Asn. The phylogenetic analysis revealed that At3g16150 and At5g08100 belong to two distinct subfamilies. The transcript levels of At3g16150 and At5g08100 were highest in sink tissues, especially in flowers and siliques, early in development, as determined by quantitative RT-PCR. The overlapping spatial patterns of expression argue for a partially redundant function of the enzymes. However, the high catalytic efficiency suggests that the K(+)-dependent enzyme may metabolize L-Asn more efficiently under conditions of high metabolic demand for N.

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“…EST DT883572 encodes the enzyme L-asparaginase (EC 3.5.1.1), a key enzyme involved in Asn hydrolysis in plants. Ammonia is released in the reaction and is utilised for the synthesis of nitrogen containing compounds, including amino acids required for protein synthesis (Casado et al 1995). EST DT883574 encodes a ketol-acid reductoisomerase (EC 1.1.1.86), an enzyme involved in synthesis of branched chain amino acids including isoleucine and valine (Dumas et al 1993 883576 encodes sulphite reductase (EC 1.8.7.1) a key enzyme of sulphate assimilation in plants (Bork et al 1998).…”

Section: Biosynthesis and Metabolismmentioning

confidence: 99%

Towards identifying the full set of genes expressed during cassava post-harvest physiological deterioration

et al. 2007

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Storage roots of cassava (Manihot esculenta Crantz) exhibit a rapid post-harvest physiological deterioration (PPD) response that can occur within 24-72 h of harvest. PPD is an enzymatically mediated oxidative process with parallels to plant wound, senescence and defence responses. To characterise those genes that show significant change in expression during the PPD response we have used cDNA microarray technology to carry out a large-scale analysis of the cassava root transcriptome during the post-harvest period. We identified 72 non-redundant expressed sequence tags which showed altered regulation during the post-harvest period. Of these 63 were induced, whilst 9 were down-regulated. RNA blot analysis of selected genes was used to verify and extend the microarray data. Additional microarray hybridisation experiments allowed the identification of 21 root-specific and 24 root-wounding-specific sequences. Many of the up-regulated and PPD-specific expressed sequence tags were predicted to play a role in cellular processes including reactive oxygen species turnover, cell wall repair, programmed cell death, ion, water or metabolite transport, signal transduction or perception, stress response, metabolism and biosynthesis, and activation of protein synthesis.

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Molecular Cloning of the Gene Encoding the L-Asparaginase Gene of Arabidopsis thaliana

Cited by 11 publications

References 4 publications

Purification and properties of asparaginase from the testa of immature seeds of pea (Pisum sativum L.)

Purification and properties of asparaginase from the testa of immature seeds of pea (Pisum sativum L.)

Co-occurrence of both l-asparaginase subtypes in Arabidopsis: At3g16150 encodes a K+-dependent l-asparaginase

Towards identifying the full set of genes expressed during cassava post-harvest physiological deterioration

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