2km8 | pdb_00002km8
Interdomain RRM packing contributes to RNA recognition in the rna15, hrp1, anchor RNA 3' processing ternary complex
Structural highlights
Function[HRP1_YEAST] RNA-binding protein, which is involved in the polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with the cleavage factor CFIA complex and the cleavage and polyadenylation factor (CPF) complex. May be involved in regulation of poly(A) site selection. Is involved in nonsense-mediated mRNA decay. Seems to bind to an RNA downstream sequence element (DSE) located 3' of a nonsense codon and may mark the transcript for decay.[1] [2] [3] [4] [RNA15_YEAST] RNA-binding component of the cleavage factor IA (CFIA) complex, which is involved in the endonucleolytic cleavage during polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with the cleavage factor NAB4/CFIB and the cleavage and polyadenylation factor (CPF) complex. Binds to A-rich RNA sequence elements.[5] [6] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedPrecise 3'-end processing of mRNA is essential for correct gene expression, yet in yeast, 3'-processing signals consist of multiple ambiguous sequence elements. Two neighboring elements upstream of the cleavage site are particularly important for the accuracy (positioning element) and efficiency (efficiency element) of 3'-processing and are recognized by the RNA-binding proteins Rna15 and Hrp1, respectively. In vivo, these interactions are strengthened by the scaffolding protein Rna14 that stabilizes their association. The NMR structure of the 34 -kDa ternary complex of the RNA recognition motif (RRM) domains of Hrp1 and Rna15 bound to this pair of RNA elements was determined by residual dipolar coupling and paramagnetic relaxation experiments. It reveals how each of the proteins binds to RNA and introduces a novel class of protein-protein contact in regions of previously unknown function. These interdomain contacts had previously been overlooked in other multi-RRM structures, although a careful analysis suggests that they may be frequently present. Mutations in the regions of these contacts disrupt 3'-end processing, suggesting that they may structurally organize the ribonucleoprotein complexes responsible for RNA processing. Novel protein-protein contacts facilitate mRNA 3'-processing signal recognition by Rna15 and Hrp1.,Leeper TC, Qu X, Lu C, Moore C, Varani G J Mol Biol. 2010 Aug 20;401(3):334-49. Epub 2010 Jun 19. PMID:20600122[7] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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