The evolutionarily conserved multifunctional glycine-rich RNA-binding proteins play key roles in development and stress adaptation

被引:77
作者
Ciuzan, Oana [1 ,2 ]
Hancock, John [3 ]
Pamfil, Doru [1 ]
Wilson, Ian [3 ]
Ladomery, Michael [3 ]
机构
[1] Univ Agr Sci & Vet Med Cluj Napoca, Cluj Napoca 400372, Romania
[2] Univ Bielefeld, Fac Biol, D-33615 Bielefeld, Germany
[3] Univ W England, Fac Hlth & Appl Sci, Bristol BS16 1QY, Avon, England
关键词
COLD-SHOCK DOMAIN; ARABIDOPSIS-THALIANA; INNATE IMMUNITY; SPLICING FACTOR; MESSENGER-RNA; FEEDBACK LOOP; ORYZA-SATIVA; EXPRESSION; ATGRP7; RECOGNITION;
D O I
10.1111/ppl.12286
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
The class IV glycine-rich RNA-binding proteins are a distinct subgroup within the heterogenous superfamily of glycine-rich proteins (GRPs). They are distinguished by the presence of an RNA-binding domain in the N-terminus; generally in the form of an RNA-recognition motif (RRM) or a cold-shock domain (CSD). These are followed by a C-terminal glycine-rich domain. Growing evidence suggests that these proteins play key roles in the adaptation of organisms to biotic and abiotic stresses including those resulting from pathogenesis, alterations in the osmotic, saline and oxidative environment and changes in temperature. Similar vertebrate proteins are also cold-induced and involved in, e.g. hibernation, suggesting evolutionarily conserved functions. The class IV RNA-binding GRPs are likely to operate as key molecular components of hormonally regulated development and to work by regulating gene expression at multiple levels by modifying alternative splicing, mRNA export, mRNA translation and mRNA degradation.
引用
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页码:1 / 11
页数:11
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