Abstract
RNA helicases of the DEAH/RHA family form a large and conserved class of enzymes that remodel RNA protein complexes (RNPs) by translocating along the RNA. Driven by ATP hydrolysis, they exert force to dissociate hybridized RNAs, dislocate bound proteins or unwind secondary structure elements in RNAs. The sub-cellular localization of DEAH-helicases and their concomitant association with different pathways in RNA metabolism, such as pre-mRNA splicing or ribosome biogenesis, can be guided by cofactor proteins that specifically recruit and simultaneously activate them. Here we review the mode of action of a large class of DEAH-specific adaptor proteins of the G-patch family. Defined only by their eponymous short glycine-rich motif, which is sufficient for helicase binding and stimulation, this family encompasses an immensely varied array of domain compositions and is linked to an equally diverse set of functions. G-patch proteins are conserved throughout eukaryotes and are even encoded within retroviruses. They are involved in mRNA, rRNA and snoRNA maturation, telomere maintenance and the innate immune response. Only recently was the structural and mechanistic basis for their helicase enhancing activity determined. We summarize the molecular and functional details of G-patch-mediated helicase regulation in their associated pathways and their involvement in human diseases.
Highlights
RNA helicases of the helicase superfamily 1 and 2 (SF1 and SF2) contribute to diverse aspects of RNA metabolism through their functions in structurally remodelling RNAs and ribonucleoprotein complexes (RNPs) (reviewed in Jarmoskaite and Russell (2014))
These nucleotide triphosphate (NTP)-dependent enzymes are characterised by a common core composed of tandem RecA-like (RecA1 and RecA2) domains that harbour conserved sequence motifs involved in RNA substrate binding, and NTP binding and hydrolysis (Caruthers and McKay 2002)
The G-patch proteins represent a heterogeneous family of proteins involved in diverse aspects of RNA metabolism
Summary
RNA helicases of the helicase superfamily 1 and 2 (SF1 and SF2) contribute to diverse aspects of RNA metabolism through their functions in structurally remodelling RNAs and ribonucleoprotein complexes (RNPs) (reviewed in Jarmoskaite and Russell (2014)). GPKOW is a phosphorylation substrate of protein kinase A and phosphorylation of GPKOW impairs its interaction with RNA, suggesting that dynamic post-translational modification may regulate GPKOW recruitment to spliceosomes and/or its functions in pre-mRNA splicing (Aksaas et al 2011).
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