Skip to main content

Research Repository

Advanced Search

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

Wilson, Ian; Hancock, John T.; Ciuzan, Oana; Wilson, Ian D.; Pamfil, Doru; Ladomery, Michael

Authors

Ian Wilson

Oana Ciuzan

Doru Pamfil



Abstract

© 2014 Scandinavian Plant Physiology Society. 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.

Journal Article Type Article
Publication Date Jan 1, 2015
Journal Physiologia Plantarum
Print ISSN 0031-9317
Electronic ISSN 1399-3054
Publisher Wiley
Peer Reviewed Peer Reviewed
Volume 153
Issue 1
Pages 1-11
APA6 Citation Wilson, I., Hancock, J., Ciuzan, O., Hancock, J. T., Pamfil, D., Wilson, I. D., & Ladomery, M. (2015). The evolutionarily conserved multifunctional glycine-rich RNA-binding proteins play key roles in development and stress adaptation. Physiologia Plantarum, 153(1), 1-11. https://doi.org/10.1111/ppl.12286
DOI https://doi.org/10.1111/ppl.12286
Keywords glycine-rich proteins, RNA-binding, stress adaptation
Publisher URL http://dx.doi.org/10.1111/ppl.12286
;