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爱丁堡大学Gary Loake教授课题组招聘博士生1名

2023/1/5 9:33:44  阅读:214 发布者:

爱丁堡大学Gary Loake教授课题组招聘博士生1

JRCEB PhD Project (浙江大学-爱丁堡大学生物学联合中心博士生项目,植物分子生物学方向)

Project Funding Details

The University of Edinburgh (UoE) and Zhejiang (ZJU) have established a Joint Centre for Engineering Biology (JCEB) in Haining, on the ZJU International campus. This project will also have some linkage to the new JCEB. The students will have one UoE and one ZJU supervisor. However, the PhD study will be located at UoE PhD, although if advantageous, it will be possible to spend some time at ZJU.  The PhD will be a UoE PhD. The difference between international and UK fee rate will be covered by the University of Edinburgh for the successful candidate. Thus, the PhD student will pay UK fees £4,500 per year for three years and not international fees £28,000 per year. So the PhD student will save: 3 x (£28,000 - £4,500) = £70,500.The student will have to fund their own accommodation and living expenses, typically ~£15,000 / year.

For further information please contact Professor Gary Loake by email (G.Loake@ed.ac.uk).

Project Title

Exploiting S-nitrosylation to establish novel strategies for improved crop traits

Project Description

The small, redox active molecule, nitric oxide (NO), is a key orchestrator of cellular signalling systems throughout eukaryotes. In plants, NO is central to the control of immunity, responses to the environment and multiple developmental programmes. A major route for the transfer of NO bioactivity is S-nitrosylation, the addition of an NO moiety to a reactive cysteine (Cys) thiol, embedded in a target protein, to form an S-nitrosothiol (SNO). This, prototypic, redox-based, post-translational modification (PTM), is conceptually similar to more established PTMs such as phosphorylation, although far less understood. In this context, S-nitrosylation can modulate protein function, for example, by regulating enzyme activity, protein localization, protein-protein interactions, protein degradation and protein-DNA binding.

Until recently, S-nitrosylation was thought to be driven largely by NO chemistry. However, now excitingly a series of enzymes are emerging, termed nitrosylases, that can add NO to specific Cys residues in target proteins, together with, de-nitrosylases, which can specifically remove these NO adducts. Thus, these enzymes are conceptually similar to kinases and phosphatases, that operate in phosphorylation and de-phosphorylation, respectively. How these enzymes exert their control over plant biology remains to be established. In addition, S-nitrosoglutathione reductase (GSNOR), constitutes an additional mechanism to control global S-nitrosylation, with loss-of-function mutations in this gene disrupting plant immunity and key aspects of development, underscoring the importance of S-nitrosylation in plant biology.

To date, these findings have been largely determined in Arabidopsis, a model dicot plant species. In this project, we will explore S-nitrosylation in the monocot crop species, rice and barley, with a view to developing novel strategies to establish crops with enhanced disease resistance and / or increased protection against environmental stress, utilising gene editing strategies to reprogramme identified target genes.

References (1 4)

1. Yun, B-W., Feechan, A., Yin, M., Saidi, N. B.B., Yu, M., Le Bihan, T. Kang, J.-G., Kwon, E., Spoel, S., Pallas, J.A. and Loake, G.J. (2011). S-nitrosylation of NADPH oxidase regulates cell death in plant immunity. Nature 478, 264-268.

2. Feechan, A., Kwon, E.-J., Yun, B.-W., Wang, Y., Pallas, J.A. and Loake, G.J. (2005). A Central Role for S-Nitrosothiols in Plant Disease Resistance. Proc. Natl. Acad. Sci. USA 102, 8054-8059.

3. Cui, B., Pan, Q., Clarke, D.,Yuan, B., Shan, W., Jiang, J-H. and Loake, G.J. (2018). S-nitrosylation of the zinc finger protein, SRG1, regulates plant immunity. Nature Comm. 9, 4226.

4. Skelly, MJ., Malik, S.I., Le Bihan, T., Bo, Y., Spoel, S.H., Jiang, J. Loake, G.J. (2019). S-nitrosylation of the SUMO-conjugating enzyme, SCE1, regulates plant immunity. Proc. Natl. Acad. Sci. USA 116, 17090-17095.

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