Enhancing protein stability with retained biological function in transgenic plants

Jang, In-C. and Niu, Q-W. and Deng, S. (2012) Enhancing protein stability with retained biological function in transgenic plants. The Plant Journal. 36 pp..

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Abstract

The final expression level of a transgene-derived protein in transgenic plants depends on transcriptional and post-transcriptional processes. Here, we focused on methods to improve protein stability without comprising biological function. We found that the 4 isoforms of the Arabidopsis RAD23 protein family are relatively stable. The UBA2 domain derived from RAD23a can be used as a portable stabilizing signal to prolong half-life of two unstable transcription factors (TFs), HFR1 and PIF3. Increased stability of the TF-UBA2 fusion protein results in an enhanced phenotype in transgenic plants as compared to expression of the TF alone. Similar results were obtained for the RAD23a UBA1domain. In addition to UBA1/2 of RAD23a, the UBA domain from the Arabidopsis DDI1 protein also could increase the half-life of the unstable protein JAZ10.1, which is involved in jasmonate signaling. Taken together, our results suggest UBA fusions can be used to increase stability of unstable proteins for basic plant biology research as well as crop improvement.

Item Type: Article
Additional Information: We thank members of the Chua lab, Drs Enno Krebbers, Barbara Mazur, Bobby Williams, Carl Falco and Brian McGonigle for useful discussions, and Dr Xiuren Zhang for Rad23b antibody. This work was supported by a grant from E. I. du Pont de Nemours and Company. PZ Zhao was supported in part by a scholarship from the Ministry of Education, China.
Uncontrolled Keywords: protein stability, RAD23, DDI1, ubiquitin-associated domain, UBA1, UBA2,Technical Advance
Author Affiliation: Laboratory of Plant Molecular Biology, The Rockefeller University, 1230 York Avenue, New York, NY 10065, USA
Subjects: Crop Improvement
Divisions: General
Depositing User: Mr Siva Shankar
Date Deposited: 30 May 2012 03:39
Last Modified: 30 May 2012 03:40
Official URL: http://dx.doi.org/10.1111/j.1365-313X.2012.05060.x
URI: http://eprints.icrisat.ac.in/id/eprint/5921

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