INVESTIGADORES
GOLDRAIJ ariel
congresos y reuniones científicas
Título:
S63-RNase is a novel non-functional S-RNase induced by phosphate starvation in Nicotiana
Autor/es:
HERNÁN ROJAS; ARIEL GOLDRAIJ
Lugar:
Potrero de Funes, San Luis
Reunión:
Congreso; XLVII Reunión Anual Sociedad Argentina de Investigación en Bioquímica y Biología Molecular; 2011
Resumen:
S63-RNase
is a novel non-functional S-RNase induced by phosphate starvation in Nicotiana
Hernán J Rojas and
Ariel Goldraij
CIQUIBIC-CONICET
Dpto. Química Biológica, Facultad de Cs. Químicas, Universidad Nacional de
Córdoba.
T2 ribonucleases
(RNases) are secretory enzymes that catalyze the cleavage of single-strand RNA.
In plants T2 RNases have different structural traits and biological roles and
were classified in two subfamilies, a) S-RNases, involved in pollen recognition
and rejection in plants with S-RNase-based self-incompatibility (SI) system and
b) S-like-RNases, widely distributed in the plant kingdom and generally
involved in the response to different biotic and abiotic stress scenarios.
We have cloned a
style cDNA from Nicotiana alata that exhibited the typical sequence features of
an S-RNase gene, but it was non-functional in the SI system and therefore, it
was denoted as non-functional S63-RNase. Surprisingly, this gene was induced when
plants were hydroponically grown without Pi, a typical response of the
S-like-RNases, but not reported yet in S-RNases or non-functional S-RNases. The
induction was detected 7 days after Pi deprivation and increased until day 22,
roughly paralleling the induction of a well-characterized S-like-RNase of
Nicotiana alata. A 15 amino acid peptide of S63-RNase was used to develop a
rabbit antibody. The antibody recognized a protein of ~31 kDa in crude extracts
of roots coming from plants grown under Pi starvation conditions only. We are
now identifying the 31 kDa protein. So far, no function has been previously
assigned to non-S-RNases.