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

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 po...

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Veröffentlicht in:Journal of experimental botany. - 1985. - 54(2003), 383 vom: 01. Feb., Seite 623-32
1. Verfasser: Zanetti, María Eugenia (VerfasserIn)
Weitere Verfasser: Blanco, Flavio Antonio, Daleo, Gustavo Raúl, Casalongué, Claudia Anahí
Format: Aufsatz
Sprache:English
Veröffentlicht: 2003
Zugriff auf das übergeordnete Werk:Journal of experimental botany
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Phosphorus Radioisotopes Plant Proteins Trans-Activators Egtazic Acid 526U7A2651 Protein Kinases EC 2.7.- Dimethyl Sulfoxide YOW8V9698H
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100 1 |a Zanetti, María Eugenia  |e verfasserin  |4 aut 
245 1 0 |a Phosphorylation of a member of the MBF1 transcriptional co-activator family, StMBF1, is stimulated in potato cell suspensions upon fungal elicitor challenge 
264 1 |c 2003 
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520 |a 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 phosphorylation assays were performed. StMBF1 is phosphorylated under both experimental conditions and [(32)P] 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 
650 4 |a Journal Article 
650 4 |a Research Support, Non-U.S. Gov't 
650 7 |a Phosphorus Radioisotopes  |2 NLM 
650 7 |a Plant Proteins  |2 NLM 
650 7 |a Trans-Activators  |2 NLM 
650 7 |a Egtazic Acid  |2 NLM 
650 7 |a 526U7A2651  |2 NLM 
650 7 |a Protein Kinases  |2 NLM 
650 7 |a EC 2.7.-  |2 NLM 
650 7 |a Dimethyl Sulfoxide  |2 NLM 
650 7 |a YOW8V9698H  |2 NLM 
700 1 |a Blanco, Flavio Antonio  |e verfasserin  |4 aut 
700 1 |a Daleo, Gustavo Raúl  |e verfasserin  |4 aut 
700 1 |a Casalongué, Claudia Anahí  |e verfasserin  |4 aut 
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