Location
University of Nevada Las Vegas, Student Union Ball Room
Start Date
6-8-2008 9:00 AM
End Date
6-8-2008 12:00 PM
Description
The WRKY super family is known to play a major role during the plant stress response and development. My project focuses on the protein-protein interaction of an Oryzasativa (rice) transcription factor, OsWRKY71 which functions as the repressor of gibberellins signaling pathway. Previous literature revealed that OsWRKY71 can interact with itself or OsWRKY51 to form dimmers by using bimolecular fluorescence complementation (BiFC). To confirm this result, we use yeast two-hybrid system. As our data showed, OsWRKY71 seems to suppress the reporter gene expression of the conventional yeast two-hybrid system, so we use a modified yeast two-hybrid, Mating-based Split Ubiquitin System (MbSUS). The result confirms OsWRKY71 can interact with another OsWRKY71, so this system can be used for future studies of protein-protein interaction of OsWRKY71. Images from Confocal microscopy show OsWRKY71 proteins are anchored on to the membrane through the membrane adaptor, and the Support Vector Machine software confirms the protein-protein interaction of OsWRKY71. The next step of this project is to construct the full length cDNA library of rice to screen suspicious proteins in a larger scale.
Keywords
Bimolecular fluorescence complementation (BiFC); Oryza sativa; Plant development; Plant stress; Protein-protein interaction; Reporter genes; Rice; WRKY proteins
Disciplines
Molecular Genetics | Plant Biology
Language
English
Decoding the protein interaction network - an approach integrating biology and math
University of Nevada Las Vegas, Student Union Ball Room
The WRKY super family is known to play a major role during the plant stress response and development. My project focuses on the protein-protein interaction of an Oryzasativa (rice) transcription factor, OsWRKY71 which functions as the repressor of gibberellins signaling pathway. Previous literature revealed that OsWRKY71 can interact with itself or OsWRKY51 to form dimmers by using bimolecular fluorescence complementation (BiFC). To confirm this result, we use yeast two-hybrid system. As our data showed, OsWRKY71 seems to suppress the reporter gene expression of the conventional yeast two-hybrid system, so we use a modified yeast two-hybrid, Mating-based Split Ubiquitin System (MbSUS). The result confirms OsWRKY71 can interact with another OsWRKY71, so this system can be used for future studies of protein-protein interaction of OsWRKY71. Images from Confocal microscopy show OsWRKY71 proteins are anchored on to the membrane through the membrane adaptor, and the Support Vector Machine software confirms the protein-protein interaction of OsWRKY71. The next step of this project is to construct the full length cDNA library of rice to screen suspicious proteins in a larger scale.
Comments
Abstract & poster