Event Title
Location
Parker-Reed, SSWAC
Start Date
1-5-2014 9:00 AM
End Date
1-5-2014 10:00 AM
Project Type
Poster
Description
Transcription factor TaABF1, a member of the ABA response element binding factor family, has been shown to have an important role in the signaling pathways of gibberellin (GA) and abscisic acid (ABA) in cereal grains. TaABF1 has also been found phosphorylated in vivo in aleurone cells and is possibly regulated by phosphatases. In order to investigate whether TaABF1 can be phosphorylated by proteins in wheat grains and which regions of the protein are phosphorylated, the GST::TaABF1 fusion protein was purified by a glutathione affinity column and a phosphorylation assay with wheat endosperm proteins was performed. Then, the possibly phosphorylated GST::TaABF1 fusion protein was purified with approximately 10-15 percent recovery for analysis with mass spectrometry.
Sponsoring Department
Colby College. Biology Dept.
CLAS Field of Study
Natural Sciences
Event Website
http://www.colby.edu/clas
ID
639
Included in
Purification of GST::TaABF1 Fusion Protein in Order to Assess its Phosphorylation by Endosperm Proteins
Parker-Reed, SSWAC
Transcription factor TaABF1, a member of the ABA response element binding factor family, has been shown to have an important role in the signaling pathways of gibberellin (GA) and abscisic acid (ABA) in cereal grains. TaABF1 has also been found phosphorylated in vivo in aleurone cells and is possibly regulated by phosphatases. In order to investigate whether TaABF1 can be phosphorylated by proteins in wheat grains and which regions of the protein are phosphorylated, the GST::TaABF1 fusion protein was purified by a glutathione affinity column and a phosphorylation assay with wheat endosperm proteins was performed. Then, the possibly phosphorylated GST::TaABF1 fusion protein was purified with approximately 10-15 percent recovery for analysis with mass spectrometry.
https://digitalcommons.colby.edu/clas/2014/program/201