Regulation of DEAH/RHA Helicases by G-Patch Proteins

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...

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Bibliographic Details
Published in:BioMed research international 2015-01, Vol.2015 (2015), p.1-9
Main Authors: Robert-Paganin, Julien, Leulliot, N., Réty, Stéphane
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Binding sites
Biomedical research
Biosynthesis
DEAD-box RNA Helicases - metabolism
G proteins
Genetic aspects
Genetic regulation
GTP-Binding Proteins - metabolism
Helicases
Humans
Life Sciences
Metabolism
Molecular Sequence Data
Mutation
Physiological aspects
Protein research
Protein Structure, Tertiary
Proteins
Review
RNA
RNA - metabolism
Sequence Alignment
Yeast
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Summary: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.
ISSN:2314-6133
2314-6141
DOI:10.1155/2015/931857