Enzyme-RNA Substrate Recognition in RNA-Modifying Enzymes

Authors: Robert Byrne (University of York) , David Waterman (Diamond Light Source) , Fred Antson (University of York)
Co-authored by industrial partner: No

Type: Book Chapter

State: Published (Approved)
Published: June 2009

Abstract: The recognition of the correct substrate and rejection of the incorrect substrate by RNA-modifying enzymes is of great importance to the process of posttranscriptional base modification. Between 2001 and 2008, structures of nine different rRNA and tRNA base-modifying enzymes in complex with RNA were published and these revealed a plethora of mechanisms for substrate recognition. While some complexes appear to be the result of the RNA being bound primarily as a rigid body, a significant number of enzymes remodel the RNA upon binding, either to increase the affinity of the interaction and/or access an otherwise buried base. Pertinent examples of remodelled RNA are observed in the structures of the ArcTGT-tRNA and RlmD-rRNA complexes. In a number of RNA-modifying enzymes it is clear that there is a degree of modularity, such that the substrate specificity is partly defined by a domain(s) that recognises a particular feature in the RNA while the modification is performed by a suitably positioned catalytic domain. With this chapter we will first review the general principles of protein-RNA interactions and modularity in RNA-modifying enzymes before looking at how they are combined to define substrate specificity in a number of interesting protein-RNA complexes.

Subject Areas: Biology and Bio-materials

Technical Areas: