The biophysical characterization of Sub1A-1, the transcription factor for rice submergence survival
Date Issued
2016
Date
2016
Author(s)
Tsai, Yu-Lin
Abstract
Due to the global warming, recent climate changes result more frequent flood and drought than the pass and becomes a serious threat to the global food security. Rice feeding over half of the population in the world and it is an emerging issue to protect rice production from weather damage. Most domesticated rice cultivars die within a week of complete submergence (flooding). However, some wild rice has a remarkable ability to withstand flood. By Genome-wide studies, it is shown that SUBMERGENCE 1 (SUB1) locus is response for the submergence resistant and the transcription factor, Sub1A-1 coded in SUB1 locus is the key factor. However, the molecular mechanism of Sub1A-1 remains unknown. Sub1A-1 is a member of group VII ethylene responsive factors (ERFVIIs) which contain an AP2 domain for GCC box (AGCCGCC) binding. More than 3,000 genes in rice genome have GCC box in their promoter region. It is virtually impossible to screen them by genetic approaches. Not to mention that there is no cell-based submergence assay. In order to narrow down its downstream targets, we have developed a binding assay by Fluorescence Polarization (FP). In addition, we have discovered that AP2 domain itself may not provide sufficient binding ability. Only with the N-terminal domain could AP2 domain of Sub1A-1 bind to DNA. This new finding could enlarge our knowledge about ERFVII family. Currently, our knowledge about ERFVII family is limited to containing one AP2 domain for DNA binding. Moreover, knowing more about Sub1A-1 protein can facilitate our Sub1A-1 and DNA co-crystallization work. Currently, we have found out several conditions which could form small crystallite. Refining these conditions may solve the 3D-structure of Sub1A-1/DNA complex which could provide solid evidence for our new finding.
Subjects
Transcription factor Sub1A-1
Submergence
Fluorescence polarization
ERFVII
Protein crystal
Type
thesis
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