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Physical interaction between 14-3-3 and neutral/alkaline invertase in Arabidopsis thaliana
Date Issued
2011
Date
2011
Author(s)
Lai, Shiuan-Jeng
Abstract
14-3-3 is a scaffold protein which regulates many protein functions such as enzyme activity and protein localization in Arabidopsis. In a previous study, 14-3-3 was found to interact with neutral invertase CINV1 by use of tandem affinity purification as a tool. We hypothesized that neutral invertase CINV1 may directly or indirectly interact with 14-3-3. Invertase catalyzes sucrose catabolism into glucose and fructose. We test and confirmed the interaction between 14-3-3omega and neutral invertase CINV1 by Bimolecular Fluorescence Complementation. This interaction may change the subcellular localization of CINV1. We have examined the phenotype of Arabidopsis cinv1 mutants under various growth condition. Our results indicate that the cinv1 mutants are salt sensitive.
Subjects
14-3-3
cytosolic invertase
Bimolecular Fluorescence Complementation
salt stress
Type
thesis
File(s)
No Thumbnail Available
Name
ntu-100-R97b42024-1.pdf
Size
23.32 KB
Format
Adobe PDF
Checksum
(MD5):f903e774fbeae077da0165077b7e8c44