2CJK

Structure of the RNA binding domain of Hrp1 in complex with RNA

Summary for 2CJK

• Entry DOI: 10.2210/pdb2cjk/pdb
• Descriptor: NUCLEAR POLYADENYLATED RNA-BINDING PROTEIN 4, 5'-R(*UP*AP*UP*AP*UP*AP*UP*AP)-3' (2 entities in total)
• Functional Keywords: hrp1, rna-binding, rna processing, mrna processing, nonsense-mediated mrna decay, cleavage, polyadenylation, nuclear protein, rna-binding protein, rna binding protein
• Biological source: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST); More
• Cellular location: Cytoplasm: Q99383
• Total number of polymer chains: 2
• Total formula weight: 21562.09

Authors

Perez-Canadillas, J.M. (deposition date: 2006-04-04, release date: 2006-06-28, Last modification date: 2024-05-15)

Primary citation

Perez-Canadillas, J.M.
Grabbing the message: structural basis of mRNA 3'UTR recognition by Hrp1.
EMBO J., 25:3167-3178, 2006

PubMed Abstract: The recognition of specific signals encoded within the 3'-untranslated region of the newly transcribed mRNA triggers the assembly of a multiprotein machine that modifies its 3'-end. Hrp1 recognises one of such signals, the so-called polyadenylation enhancement element (PEE), promoting the recruitment of other polyadenylation factors in yeast. The molecular bases of this interaction are revealed here by the solution structure of a complex between Hrp1 and an oligonucleotide mimicking the PEE. Six consecutive bases (AUAUAU) are specifically recognised by two RNA-binding domains arranged in tandem. Both protein and RNA undergo significant conformational changes upon complex formation with a concomitant large surface burial of RNA bases. Key aspects of RNA specificity can be explained by the presence of intermolecular aromatic-aromatic contacts and hydrogen bonds. Altogether, the Hrp1-PEE structure represents one of the first steps towards understanding of the assembly of the cleavage and polyadenylation machinery at the atomic level.

PubMed: 16794580
DOI: 10.1038/sj.emboj.7601190

Experimental method

SOLUTION NMR