Display Settings:


Send to:

Choose Destination
We are sorry, but NCBI web applications do not support your browser and may not function properly. More information
Mol Biol Rep. 2009 Nov;36(8):2249-58. doi: 10.1007/s11033-008-9441-y. Epub 2009 Jan 6.

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

Author information

  • 1Departamento de Botánica, Ecología y Fisiología Vegetal, Instituto Andaluz de Biotecnología, Universidad de Córdoba, Campus de Rabanales, Edif. C-4, 3a Planta, 14071 Córdoba, Spain.


A gene encoding a putative asparagine synthetase (AS; EC 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.

[PubMed - indexed for MEDLINE]
PubMed Commons home

PubMed Commons

How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Springer
    Loading ...
    Write to the Help Desk