5VZJ

STRUCTURE OF A TWELVE COMPONENT MPP6-NUCLEAR RNA EXOSOME COMPLEX BOUND TO RNA

Summary for 5VZJ

• Entry DOI: 10.2210/pdb5vzj/pdb
• Descriptor: Exosome complex component RRP45, Exosome complex exonuclease RRP6, Exosome complex exonuclease DIS3, ... (18 entities in total)
• Functional Keywords: exoribonuclease, complex, rna, structural protein, hydrolase-rna complex, hydrolase/rna
• Biological source: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast); More
• Total number of polymer chains: 14
• Total formula weight: 479983.22

Authors

Lima, C.D.,Wasmuth, E.V. (deposition date: 2017-05-28, release date: 2017-08-02, Last modification date: 2023-10-04)

Primary citation

Wasmuth, E.V.,Zinder, J.C.,Zattas, D.,Das, M.,Lima, C.D.
Structure and reconstitution of yeast Mpp6-nuclear exosome complexes reveals that Mpp6 stimulates RNA decay and recruits the Mtr4 helicase.
Elife, 6:-, 2017

PubMed Abstract: Nuclear RNA exosomes catalyze a range of RNA processing and decay activities that are coordinated in part by cofactors, including Mpp6, Rrp47, and the Mtr4 RNA helicase. Mpp6 interacts with the nine-subunit exosome core, while Rrp47 stabilizes the exoribonuclease Rrp6 and recruits Mtr4, but it is less clear if these cofactors work together. Using biochemistry with proteins, we show that Rrp47 and Mpp6 stimulate exosome-mediated RNA decay, albeit with unique dependencies on elements within the nuclear exosome. Mpp6-exosomes can recruit Mtr4, while Mpp6 and Rrp47 each contribute to Mtr4-dependent RNA decay, with maximal Mtr4-dependent decay observed with both cofactors. The 3.3 Å structure of a twelve-subunit nuclear Mpp6 exosome bound to RNA shows the central region of Mpp6 bound to the exosome core, positioning its Mtr4 recruitment domain next to Rrp6 and the exosome central channel. Genetic analysis reveals interactions that are largely consistent with our model.

PubMed: 28742025
DOI: 10.7554/eLife.29062

Experimental method

X-RAY DIFFRACTION (3.3 Å)