INVESTIGADORES
BLANCO Flavio Antonio
artículos
Título:
Phosphorylation of a member of the MBF1 transcriptional co-activator family, StMBF1, is stimulated in potato cell suspensions upon fungal elicitor challenge
Autor/es:
ZANETTI ME, BLANCO F, DALEO G AND CASALONGUÉ C.
Revista:
JOURNAL OF EXPERIMENTAL BOTANY
Editorial:
OXFORD UNIV PRESS
Referencias:
Año: 2003 vol. 54 p. 623 - 632
ISSN:
0022-0957
Resumen:
StMBF1 (Solanum tuberosum multiprotein bridging
factor 1) is a plant member of the MBF1 family of
transcriptional co-activators. Previously, it has been
described as being up-regulated at the transcriptional
level by fungal and abiotic stress. To understand
whether StMBF1 is also regulated at the post--
translational level, in vitro as well as in vivo
MBF1 (Solanum tuberosum multiprotein bridging
factor 1) is a plant member of the MBF1 family of
transcriptional co-activators. Previously, it has been
described as being up-regulated at the transcriptional
level by fungal and abiotic stress. To understand
whether StMBF1 is also regulated at the post--
translational level, in vitro as well as in vivo
StMBF1 is also regulated at the post--
translational level, in vitro as well as in vivoin vitro as well as in vivo
phosphorylation assays were performed. StMBF1 is
phosphorylated under both experimental conditions
and [32P] incorporation into StMBF1 increases after
treatment of potato cells with hyphal cell wall
components (HWC) derived from Phytophthora
infestans. The StMBF1-phosphorylating activity is
strongly inhibited by the calcium-chelator EGTA and
partially inhibited by calmodulin antagonists. Using
bacterial puri®ed StMBF1 as a substrate, a 57 kDa
calcium-dependent protein kinase (p57) that is able
to phosphorylate StMBF1 was detected. The StMBF1
kinase activity of p57 was higher in elicited than in
non-treated cells. The role of the elicitor-dependent
phosphorylation of StMBF1 is discussed.
StMBF1 is
phosphorylated under both experimental conditions
and [32P] incorporation into StMBF1 increases after
treatment of potato cells with hyphal cell wall
components (HWC) derived from Phytophthora
infestans. The StMBF1-phosphorylating activity is
strongly inhibited by the calcium-chelator EGTA and
partially inhibited by calmodulin antagonists. Using
bacterial puri®ed StMBF1 as a substrate, a 57 kDa
calcium-dependent protein kinase (p57) that is able
to phosphorylate StMBF1 was detected. The StMBF1
kinase activity of p57 was higher in elicited than in
non-treated cells. The role of the elicitor-dependent
phosphorylation of StMBF1 is discussed.
32P] incorporation into StMBF1 increases after
treatment of potato cells with hyphal cell wall
components (HWC) derived from Phytophthora
infestans. The StMBF1-phosphorylating activity is
strongly inhibited by the calcium-chelator EGTA and
partially inhibited by calmodulin antagonists. Using
bacterial puri®ed StMBF1 as a substrate, a 57 kDa
calcium-dependent protein kinase (p57) that is able
to phosphorylate StMBF1 was detected. The StMBF1
kinase activity of p57 was higher in elicited than in
non-treated cells. The role of the elicitor-dependent
phosphorylation of StMBF1 is discussed.
Phytophthora
infestans. The StMBF1-phosphorylating activity is
strongly inhibited by the calcium-chelator EGTA and
partially inhibited by calmodulin antagonists. Using
bacterial puri®ed StMBF1 as a substrate, a 57 kDa
calcium-dependent protein kinase (p57) that is able
to phosphorylate StMBF1 was detected. The StMBF1
kinase activity of p57 was higher in elicited than in
non-treated cells. The role of the elicitor-dependent
phosphorylation of StMBF1 is discussed.
. The StMBF1-phosphorylating activity is
strongly inhibited by the calcium-chelator EGTA and
partially inhibited by calmodulin antagonists. Using
bacterial puri®ed StMBF1 as a substrate, a 57 kDa
calcium-dependent protein kinase (p57) that is able
to phosphorylate StMBF1 was detected. The StMBF1
kinase activity of p57 was higher in elicited than in
non-treated cells. The role of the elicitor-dependent
phosphorylation of StMBF1 is discussed.
StMBF1 as a substrate, a 57 kDa
calcium-dependent protein kinase (p57) that is able
to phosphorylate StMBF1 was detected. The StMBF1
kinase activity of p57 was higher in elicited than in
non-treated cells. The role of the elicitor-dependent
phosphorylation of StMBF1 is discussed.
StMBF1 was detected. The StMBF1
kinase activity of p57 was higher in elicited than in
non-treated cells. The role of the elicitor-dependent
phosphorylation of StMBF1 is discussed.StMBF1 is discussed.