Yamasaki, Yuji , Randall, Stephen .
The analysis of vegetative dehydrin-like proteins in soybean.
Dehydrins, type II late embryogenesis abundant (LEA) proteins, are extremely hydrophilic proteins. They have at least one conservative lysine rich region, called K-domain and may have possible phosphorylation sites in the S-domain. Some of them are upregulated by environmental stresses such as cold and drought through the CBF dependent pathway in Arabidopsis thaliana. The increases in plant tolerance to cold or drought due to dehydrins are through unknown mechanism. Some of their biochemical characteristics reported including phosphorylation dependent Ca2+ binding activity, inhibition of lipid peroxidation, and protein chaperone activity. In soybean, we have identified 8 dehydrin-like proteins based upon expressed transcripts. We have found several possible dehydrin proteins in the vegetative stage of soybean by protein analysis using the anti K domain antibody or anti specific Arabidopsis dehydrin antibodies. These dehydrin like proteins are not expressed in the seed stage making them different than Mat9 or AS26K. They are expressed in stems and roots, higher than in leaves, and are not shown to be induced by cold stress. These vegetative dehydrins have been purified using their unique characteristics, such as heat stability and cation-binding activity. Interestingly, these purified proteins show dephosphorylation regulated apparent mass shifts on SDS-PAGE analysis like some of Arabidopsis acidic dehydrins which have been characterized to the phosphorylation dependent cation-binding activity. We are presently working on obtaining MALDI-TOF analysis of these proteins, so to identify the genes encoding them.
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1 - Indiana University Purdue University Indianapolis, Biology, 723 W. Michigan St, Indianapolis, IN, 46202, USA
2 - Indiana University Purdue University Indianapolis, Biology
Presentation Type: Plant Biology Abstract
Location: Exhibit Hall (Northeast, Southwest & Southeast)/Hilton
Date: Sunday, July 8th, 2007
Time: 8:00 AM