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

Ciuzan O, Hancock J, Pamfil D, Wilson I, Ladomery M (2015)
Physiologia Plantarum 153(1): 1-11.

Zeitschriftenaufsatz | Veröffentlicht | Englisch
 
Download
Es wurden keine Dateien hochgeladen. Nur Publikationsnachweis!
Autor*in
Ciuzan, Oana; Hancock, John; Pamfil, Doru; Wilson, Ian; Ladomery, Michael
Abstract / Bemerkung
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. © 2014 Scandinavian Plant Physiology Society.
Erscheinungsjahr
2015
Zeitschriftentitel
Physiologia Plantarum
Band
153
Ausgabe
1
Seite(n)
1-11
ISSN
0031-9317
eISSN
1399-3054
Page URI
https://pub.uni-bielefeld.de/record/2710002

Zitieren

Ciuzan O, Hancock J, Pamfil D, Wilson I, Ladomery M. The evolutionarily conserved multifunctional glycine-rich RNA-binding proteins play key roles in development and stress adaptation. Physiologia Plantarum. 2015;153(1):1-11.
Ciuzan, O., Hancock, J., Pamfil, D., Wilson, I., & 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. doi:10.1111/ppl.12286
Ciuzan, O., Hancock, J., Pamfil, D., Wilson, I., and Ladomery, M. (2015). The evolutionarily conserved multifunctional glycine-rich RNA-binding proteins play key roles in development and stress adaptation. Physiologia Plantarum 153, 1-11.
Ciuzan, O., et al., 2015. The evolutionarily conserved multifunctional glycine-rich RNA-binding proteins play key roles in development and stress adaptation. Physiologia Plantarum, 153(1), p 1-11.
O. Ciuzan, et al., “The evolutionarily conserved multifunctional glycine-rich RNA-binding proteins play key roles in development and stress adaptation”, Physiologia Plantarum, vol. 153, 2015, pp. 1-11.
Ciuzan, O., Hancock, J., Pamfil, D., Wilson, I., Ladomery, M.: The evolutionarily conserved multifunctional glycine-rich RNA-binding proteins play key roles in development and stress adaptation. Physiologia Plantarum. 153, 1-11 (2015).
Ciuzan, Oana, Hancock, John, Pamfil, Doru, Wilson, Ian, and Ladomery, Michael. “The evolutionarily conserved multifunctional glycine-rich RNA-binding proteins play key roles in development and stress adaptation”. Physiologia Plantarum 153.1 (2015): 1-11.

5 Zitationen in Europe PMC

Daten bereitgestellt von Europe PubMed Central.

Physiological Analysis and Proteome Quantification of Alligator Weed Stems in Response to Potassium Deficiency Stress.
Li LQ, Lyu CC, Li JH, Tong Z, Lu YF, Wang XY, Ni S, Yang SM, Zeng FC, Lu LM., Int J Mol Sci 20(1), 2019
PMID: 30626112
TRPV4-dependent induction of a novel mammalian cold-inducible protein SRSF5 as well as CIRP and RBM3.
Fujita T, Higashitsuji H, Higashitsuji H, Liu Y, Itoh K, Sakurai T, Kojima T, Kandori S, Nishiyama H, Fukumoto M, Fukumoto M, Shibasaki K, Fujita J., Sci Rep 7(1), 2017
PMID: 28536481
Cold-inducible proteins CIRP and RBM3, a unique couple with activities far beyond the cold.
Zhu X, Bührer C, Wellmann S., Cell Mol Life Sci 73(20), 2016
PMID: 27147467

Export

Markieren/ Markierung löschen
Markierte Publikationen

Open Data PUB

Web of Science

Dieser Datensatz im Web of Science®

Quellen

PMID: 25243592
PubMed | Europe PMC

Suchen in

Google Scholar