2KM8

Interdomain RRM packing contributes to RNA recognition in the rna15, hrp1, anchor RNA 3' processing ternary complex

Summary for 2KM8

• Entry DOI: 10.2210/pdb2km8/pdb
• NMR Information: BMRB: 16425
• Descriptor: 5'-R(P*UP*AP*UP*AP*UP*AP*UP*AP*AP*UP*AP*AP*U)-3', mRNA 3'-end-processing protein RNA15, Nuclear polyadenylated RNA-binding protein 4 (3 entities in total)
• Functional Keywords: 3' processing, rrm domain, rna15p, hrp1p, enhancer element, positioning element, rna recognition, mrna processing, nucleus, rna-binding, nonsense-mediated mrna decay, phosphoprotein, rna binding protein-rna complex, rna binding protein/rna
• Biological source: Saccharomyces cerevisiae (yeast); More
• Total number of polymer chains: 3
• Total formula weight: 32512.52

Authors

Leeper, T.C.,Varani, G. (deposition date: 2009-07-24, release date: 2010-07-28, Last modification date: 2024-05-08)

Primary citation

Leeper, T.C.,Qu, X.,Lu, C.,Moore, C.,Varani, G.
Novel Protein-Protein Contacts Facilitate mRNA 3'-Processing Signal Recognition by Rna15 and Hrp1.
J.Mol.Biol., 401:334-349, 2010

PubMed Abstract: Precise 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.

PubMed: 20600122
DOI: 10.1016/j.jmb.2010.06.032

Experimental method

SOLUTION NMR