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BioMed Research International
Volume 2015 (2015), Article ID 931857, 9 pages
http://dx.doi.org/10.1155/2015/931857
Review Article

Regulation of DEAH/RHA Helicases by G-Patch Proteins

Laboratoire de Cristallographie et RMN Biologiques, UMR CNRS 8015, Faculté des Sciences Pharmaceutiques et Biologiques, Université Paris Descartes, Sorbonne Paris-Cité, 4 avenue de l’Observatoire, 75270 Paris Cedex 06, France

Received 20 June 2014; Revised 19 October 2014; Accepted 24 October 2014

Academic Editor: Huangen Ding

Copyright © 2015 Julien Robert-Paganin et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Abstract

RNA helicases from the DEAH/RHA family are present in all the processes of RNA metabolism. The function of two helicases from this family, Prp2 and Prp43, is regulated by protein partners containing a G-patch domain. The G-patch is a glycine-rich domain discovered by sequence alignment, involved in protein-protein and protein-nucleic acid interaction. Although it has been shown to stimulate the helicase’s enzymatic activities, the precise role of the G-patch domain remains unclear. The role of G-patch proteins in the regulation of Prp43 activity has been studied in the two biological processes in which it is involved: splicing and ribosome biogenesis. Depending on the pathway, the activity of Prp43 is modulated by different G-patch proteins. A particular feature of the structure of DEAH/RHA helicases revealed by the Prp43 structure is the OB-fold domain in C-terminal part. The OB-fold has been shown to be a platform responsible for the interaction with G-patch proteins and RNA. Though there is still no structural data on the G-patch domain, in the current model, the interaction between the helicase, the G-patch protein, and RNA leads to a cooperative binding of RNA and conformational changes of the helicase.