Event Title

The Effect of Phosphorylation on Transcription Factor TaABF1’s Ability to Downregulate the Amy32b gene in Cereal Aleurone

Presenter Information

Alison Smith, Colby CollegeFollow

Location

Diamond 153

Start Date

1-5-2014 1:00 PM

End Date

1-5-2014 2:50 PM

Project Type

Presentation

Description

The transcription factor TaABF1 plays an important role in mediating hormone-induced changes in gene expression in cereal grains, allowing for seeds to respond properly to varying environmental conditions. It is necessary for the abscisic acid-induced suppression of Amy32b, a gene encoding an α-amylase in cereal grains, such as wheat and barley. In order to examine the relevance of the phosphorylation state of TaABF1 in its ability to downregulate Amy32b, we generated mutant TaABF1 constructs with aspartate or alanine substituted for serines in conserved regions in the protein to mimic the presence or absence of phosphate. Through particle bombardment, it was determined that phosphorylation at conserved region one enhances TaABF1s ability to inhibit expression of Amy32b compared to the unmodified wild-type transcription factor.

Faculty Sponsor

Cathy Bevier

Sponsoring Department

Colby College. Biology Dept.

CLAS Field of Study

Natural Sciences

Event Website

http://www.colby.edu/clas

ID

443

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May 1st, 1:00 PM May 1st, 2:50 PM

The Effect of Phosphorylation on Transcription Factor TaABF1’s Ability to Downregulate the Amy32b gene in Cereal Aleurone

Diamond 153

The transcription factor TaABF1 plays an important role in mediating hormone-induced changes in gene expression in cereal grains, allowing for seeds to respond properly to varying environmental conditions. It is necessary for the abscisic acid-induced suppression of Amy32b, a gene encoding an α-amylase in cereal grains, such as wheat and barley. In order to examine the relevance of the phosphorylation state of TaABF1 in its ability to downregulate Amy32b, we generated mutant TaABF1 constructs with aspartate or alanine substituted for serines in conserved regions in the protein to mimic the presence or absence of phosphate. Through particle bombardment, it was determined that phosphorylation at conserved region one enhances TaABF1s ability to inhibit expression of Amy32b compared to the unmodified wild-type transcription factor.

http://digitalcommons.colby.edu/clas/2014/program/27