IBR   13079
INSTITUTO DE BIOLOGIA MOLECULAR Y CELULAR DE ROSARIO
Unidad Ejecutora - UE
congresos y reuniones científicas
Título:
Identification of a new gdh gene in Solanum lycopersicum
Autor/es:
FERRARO G., MORTERA P., VALLE E.
Lugar:
Carlos Paz
Reunión:
Congreso; SAIB 2008; 2008
Institución organizadora:
SAIB
Resumen:
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Glutamate dehydrogenase (GDH)
catalyses a reversible reaction for the reductive amination of α-ketoglutarate to glutamate. Although GDH is
ubiquitous in plant tissues, its physiological role is a subject of
controversy. GDH is a hexamer comprised of two subunit polypeptides α and β,
that differ slightly in mass and charge. The association of both subunits
yields seven possible GDH isoenzymes. In several plant species these subunits
are encoded by at least two distinct genes, however in tomato (Solanum lycopersicum) only one gene, coding
for the β subunit (SlgdhB), was isolated.
Looking for others functional gdh genes in tomato, we searched in the
transcript and genomic sequences available at Sol Genomic Network database (www.sgn.cornell.edu). We found a
complete cDNA of 1604 bp, with a 56.9 % of identity to SlgdhB. This
clone was highly similar to the genes encoding the α subunit of N.
plumbaginifolia (87%) and N.
tabacum (88%). We isolated the corresponding SlgdhA putative promoter
and analyzed the predictive cis-acting elements. The expression of gdhB and gdhA was studied by real time PCR and western
blot analysis using antibodies that recognizes both subunits or only the α
subunit. We found that the expression
of both gdh genes and the isoenzyme profile were
diverse in the different tomato tissues. These data suggest that gdhB and gdhA are independently regulated in tomato
plants.