4WFD

Structure of the Rrp6-Rrp47-Mtr4 interaction

Summary for 4WFD

• Entry DOI: 10.2210/pdb4wfd/pdb
• Descriptor: Exosome complex exonuclease RRP6, Exosome complex protein LRP1, ATP-dependent RNA helicase DOB1, ... (5 entities in total)
• Functional Keywords: rrp6-rrp47 complex, nuclear exosome, rna degradation, rna processing, hydrolase
• Biological source: Saccharomyces cerevisiae (Baker's yeast); More
• Cellular location: Nucleus, nucleolus : Q12149; Nucleus : P38801 P47047
• Total number of polymer chains: 9
• Total formula weight: 83555.39

Authors

Schuch, B.,Conti, E. (deposition date: 2014-09-14, release date: 2014-10-29, Last modification date: 2024-01-10)

Primary citation

Schuch, B.,Feigenbutz, M.,Makino, D.L.,Falk, S.,Basquin, C.,Mitchell, P.,Conti, E.
The exosome-binding factors Rrp6 and Rrp47 form a composite surface for recruiting the Mtr4 helicase.
Embo J., 33:2829-2846, 2014

PubMed Abstract: The exosome is a conserved multi-subunit ribonuclease complex that functions in 3' end processing, turnover and surveillance of nuclear and cytoplasmic RNAs. In the yeast nucleus, the 10-subunit core complex of the exosome (Exo-10) physically and functionally interacts with the Rrp6 exoribonuclease and its associated cofactor Rrp47, the helicase Mtr4 and Mpp6. Here, we show that binding of Mtr4 to Exo-10 in vitro is dependent upon both Rrp6 and Rrp47, whereas Mpp6 binds directly and independently of other cofactors. Crystallographic analyses reveal that the N-terminal domains of Rrp6 and Rrp47 form a highly intertwined structural unit. Rrp6 and Rrp47 synergize to create a composite and conserved surface groove that binds the N-terminus of Mtr4. Mutation of conserved residues within Rrp6 and Mtr4 at the structural interface disrupts their interaction and inhibits growth of strains expressing a C-terminal GFP fusion of Mtr4. These studies provide detailed structural insight into the interaction between the Rrp6-Rrp47 complex and Mtr4, revealing an important link between Mtr4 and the core exosome.

PubMed: 25319414
DOI: 10.15252/embj.201488757

Experimental method

X-RAY DIFFRACTION (2.4 Å)