Getting to the end of RNA: Structural analysis of protein recognition of 5′ and 3′ termini

• Published in: Biochimica et biophysica acta Vol. 1789; no. 9; pp. 653 - 666
• Main Authors: Curry, Stephen, Kotik-Kogan, Olga, Conte, Maria R., Brick, Peter
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.09.2009
• Subjects: 3′-terminus; 5′-terminus; Animals; Autoantigens - chemistry; Crystallography, X-Ray - methods; Endoribonucleases - chemistry; Eukaryotic Initiation Factor-4E - chemistry; Humans; Models, Molecular; Molecular Conformation; NMR; Nucleic Acid Conformation; Protein crystallography; Protein Structure, Tertiary; Protein–RNA interaction; Ribonucleoproteins - chemistry; RNA; RNA - chemistry; RNA - genetics; RNA Interference; RNA maturation; Rotavirus - genetics; SS-B Antigen; Translational control; Viral Nonstructural Proteins - chemistry; Viral Proteins - chemistry; RNA maturation; NMR; RNA interference; RNA; Protein crystallography; 3′-terminus; Protein–RNA interaction; 5′-terminus; Translational control
• ISSN: 1874-9399; 0006-3002; 1876-4320
• DOI: 10.1016/j.bbagrm.2009.07.003

The specific recognition by proteins of the 5′ and 3′ ends of RNA molecules is an important facet of many cellular processes, including RNA maturation, regulation of translation initiation and control of gene expression by degradation and RNA interference. The aim of this review is to survey recent structural analyses of protein binding domains that specifically bind to the extreme 5′ or 3′ termini of RNA. For reasons of space and because their interactions are also governed by catalytic considerations, we have excluded enzymes that modify the 5′ and 3′ extremities of RNA. It is clear that there is enormous structural diversity among the proteins that have evolved to bind to the ends of RNA molecules. Moreover, they commonly exhibit conformational flexibility that appears to be important for binding and regulation of the interaction. This flexibility has sometimes complicated the interpretation of structural results and presents significant challenges for future investigations.