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Journal of Experimental Botany, Vol. 54, No. 383, pp. 623-632, February 1, 2003
© 2003 Oxford University Press

Phosphorylation of a member of the MBF1 transcriptional co-activator family, StMBF1, is stimulated in potato cell suspensions upon fungal elicitor challenge

Received 13 June 2002; Accepted 24 September 2002

María Eugenia Zanetti, Flavio Antonio Blanco, Gustavo Raúl Daleo and Claudia Anahí Casalongué1,

Instituto de Investigaciones Biológicas-Departamento de Biología, Universidad Nacional de Mar del Plata, Funes 3250, CC 1245, 7600 Mar del Plata, Argentina

1 To whom correspondence should be addressed. Fax: +54 223 4753150. E-mail: casalong{at}mdp.edu.ar
Abbreviations: aa, amino acid; CaMK, calmodulin-dependent protein kinase; CKII, casein kinase II; CDPK, calcium-dependent protein kinase; CPZ, chlorpromazine; DRB, 5,6-dichloro-1-(ß-D-ribofuranosyl); GST, glutathione-S-transferase; HWC, hyphal cell wall components; IPTG, isopropyl-1-thio-ß-D-galactopyranoside; MBF1, multiprotein bridging factor 1; PAGE, polyacrylamide gel electrophoresis; PKC, protein kinase C; TFP, trifluoperazine.

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 transcrip tional 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 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 purified 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.

Key words: Calcium-dependent protein kinase, cell suspensions, elicitor, multiprotein bridging factor 1, protein phosphorylation, Phytophthora infestans, Solanum tuberosum, transcriptional co-activator.


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