Ubiquitination: a tool for plant adaptation to changing environments

被引：14
作者：
Mandal A. [1 ,2 ]
Sharma N. [2 ]
Muthamilarasan M. [2 ,3 ]
Prasad M. [2 ]
机构：
[1] Department of Biotechnology, Maulana Abul Kalam Azad University of Technology, Kolkata, 700064, West Bengal
[2] National Institute of Plant Genome Research, Aruna Asaf Ali Marg, New Delhi
[3] ICAR-National Research Centre on Plant Biotechnology, Pusa Campus, New Delhi
来源：
The Nucleus | 2018年 / 61卷 / 3期
关键词：
Abiotic stress; Adaptation; Biotic stress; E3; ligase; Plants; Ubiquitination;
D O I：
10.1007/s13237-018-0255-6
中图分类号：
学科分类号：
摘要：
Post-translational modifications namely ubiquitination, phosphorylation, methylation and acetylation play distinct roles in regulating the growth and development of plants. Among these, the ubiquitination regulates the abundance, activities, subcellular compartmentalization and trafficking of regulatory proteins involved in diverse developmental as well as stress-responsive processes. The ubiquitin–proteasome system (UPS) involves five essential components namely ubiquitin, ubiquitin-activating enzyme (E1), ubiquitin-conjugating enzyme (E2), ubiquitin ligase (E3) and the intact 26S proteasome. The E3 ubiquitin ligase is the major component of UPS that recognizes and tethers poly-ubiquitins on the target proteins. Owing to its specificity of substrate recognition, the E3 ubiquitin ligase contributes not only to the proteome plasticity of the cell but also regulates the plant’s response to environmental cues. In this context, the review summarizes the components involved in UPS and elaborates the role of E3 ubiquitin ligase in biotic and abiotic stress responses. © 2018, Archana Sharma Foundation of Calcutta.
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页码：253 / 260
页数：7
相关论文
共 82 条
[1]  
Adams E.H.S., Spoel S.H., The ubiquitin–proteasome system as a transcriptional regulator of plant immunity, J Exp Bot, 69, pp. 4529-4537, (2018)
[2]  
Adler G., Konrad Z., Zamir L., Mishra A.K., Raveh D., Bar-Zvi D., The Arabidopsis paralogs, PUB46 and PUB48, encoding U-box E3 ubiquitin ligases, are essential for plant response to drought stress, BMC Plant Biol, 17, (2017)
[3]  
Alexandersson E., Fraysse L., Sjovall-Larsen S., Gustavsson S., Fellert M., Karlsson M., Et al., Whole gene family expression and drought stress regulation of aquaporins, Plant Mol Biol, 59, pp. 469-484, (2005)
[4]  
Aragon W., Reina-Pinto J.J., Serrano M., The intimate talk between plants and microorganisms at the leaf surface, J Exp Bot, 68, pp. 5339-5350, (2017)
[5]  
Aravind L., Koonin E.V., The U box is a modified RING finger—a common domain in ubiquitination, Curr Biol, 10, pp. R132-R134, (2000)
[6]  
Azevedo C., Santos-Rosa M.J., Shirasu K., The U-box protein family in plants, Trends Plant Sci, 6, pp. 354-358, (2001)
[7]  
Blanc C., Coluccia F., L'Haridon F., Torres M., Ortiz-Berrocal M., Stahl E., Et al., The cuticle mutant eca2 modifies plant defense responses to biotrophic and necrotrophic pathogens and herbivory insects, Mol Plant Microbe Interact, 31, pp. 344-355, (2018)
[8]  
Bonas U., Lahaye T., Plant disease resistance triggered by pathogen-derived molecules: refined models of specific recognition, Curr Opin Microbiol, 5, pp. 44-50, (2002)
[9]  
Boyes D.C., Nam J., Dangl J.L., The Arabidopsis thaliana RPM1 disease resistance gene product is a peripheral plasma membrane protein that is degraded coincident with the hypersensitive response, Proc Natl Acad Sci USA, 95, pp. 15849-15854, (1998)
[10]  
Callis J., Carpenter T., Sun C.W., Vierstra R.D., Structure and evolution of genes encoding polyubiquitin and ubiquitin-like proteins in Arabidopsis thaliana ecotype Columbia, Genetics, 139, pp. 921-939, (1995)
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