CryoEM structure of yeast cytoplasmic exosome complex View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2016-07

AUTHORS

Jun-Jie Liu, Chu-Ya Niu, Yao Wu, Dan Tan, Yang Wang, Ming-Da Ye, Yang Liu, Wenwei Zhao, Ke Zhou, Quan-Sheng Liu, Junbiao Dai, Xuerui Yang, Meng-Qiu Dong, Niu Huang, Hong-Wei Wang

ABSTRACT

The eukaryotic multi-subunit RNA exosome complex plays crucial roles in 3'-to-5' RNA processing and decay. Rrp6 and Ski7 are the major cofactors for the nuclear and cytoplasmic exosomes, respectively. In the cytoplasm, Ski7 helps the exosome to target mRNAs for degradation and turnover via a through-core pathway. However, the interaction between Ski7 and the exosome complex has remained unclear. The transaction of RNA substrates within the exosome is also elusive. In this work, we used single-particle cryo-electron microscopy to solve the structures of the Ski7-exosome complex in RNA-free and RNA-bound forms at resolutions of 4.2 Å and 5.8 Å, respectively. These structures reveal that the N-terminal domain of Ski7 adopts a structural arrangement and interacts with the exosome in a similar fashion to the C-terminal domain of nuclear Rrp6. Further structural analysis of exosomes with RNA substrates harboring 3' overhangs of different length suggests a switch mechanism of RNA-induced exosome activation in the through-core pathway of RNA processing. More... »

PAGES

822

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/cr.2016.56

DOI

http://dx.doi.org/10.1038/cr.2016.56

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1004924311

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/27174052


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