PVAS3, a class-II ubiquitous asparagine synthetase from the common bean (Phaseolus vulgaris)

A gene encoding a putative asparagine synthetase (AS; EC 6.3.5.4) has been isolated from common bean (Phaseolus vulgaris). A 2.4 kb cDNA clone of this gene (PVAS3) encodes a protein of 570 amino acids with a predicted molecular mass of 64,678 Da, an isoelectric point of 6.45, and a net charge of −5....

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Published inMolecular biology reports Vol. 36; no. 8; pp. 2249 - 2258
Main Authors Parra-Peralbo, Esmeralda, Pineda, Manuel, Aguilar, Miguel
Format Journal Article
LanguageEnglish
Published Dordrecht Dordrecht : Springer Netherlands 01.11.2009
Springer Netherlands
Springer Nature B.V
Subjects
Amino Acid Sequence
Amino acids
Animal Anatomy
Animal Biochemistry
Aspartate-Ammonia Ligase - chemistry
Aspartate-Ammonia Ligase - genetics
Aspartate-Ammonia Ligase - metabolism
Biomedical and Life Sciences
Cloning, Molecular - methods
Comparative studies
Escherichia coli - genetics
Gene expression
Genes, Plant
Genetic Complementation Test
Histology
Legumes
Life Sciences
Molecular biology
Molecular Sequence Data
Morphology
Phaseolus - enzymology
Phaseolus - genetics
Phylogeny
Polymerase Chain Reaction
Promoter Regions, Genetic
Sequence Alignment
Tissue Distribution
Asparagine synthetase
Phaseolus vulgaris
Legume
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Summary:A gene encoding a putative asparagine synthetase (AS; EC 6.3.5.4) has been isolated from common bean (Phaseolus vulgaris). A 2.4 kb cDNA clone of this gene (PVAS3) encodes a protein of 570 amino acids with a predicted molecular mass of 64,678 Da, an isoelectric point of 6.45, and a net charge of −5.9 at pH 7.0. The PVAS3 protein sequence conserves all the amino acid residues that are essential for glutamine-dependent AS, and PVAS3 complemented an E. coli asparagine auxotroph, that demonstrates that it encodes a glutamine-dependent AS. PVAS3 displayed significant similarity to other AS. It showed the highest similarity to soybean SAS3 (92.9% identity), rice AS (73.7% identity), Arabidopsis ASN2 (73.2%) and sunflower HAS2 (72.9%). A phylogenetic analysis revealed that PVAS3 belongs to class-II asparagine synthetases. Expression analysis by real-time RT-PCR revealed that PVAS3 is expressed ubiquitously and is not repressed by light.
Bibliography:http://dx.doi.org/10.1007/s11033-008-9441-y
ISSN:0301-4851
1573-4978
DOI:10.1007/s11033-008-9441-y