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From Proteopedia
Structure of the Nop53 pre-60S particle bound to the exosome nuclear cofactors
Structural highlights
FunctionPublication Abstract from PubMedThe RNA exosome complex processes and degrades a wide range of transcripts, including ribosomal RNAs. We used cryo-EM to visualize the yeast nuclear exosome holo-complex captured on a precursor large ribosomal subunit (pre-60S) during 7S-to-5.8S rRNA processing. The cofactors of the nuclear exosome are sandwiched between the ribonuclease core complex (Exo-10) and the remodeled "foot" structure of the pre-60S particle, which harbors the 5.8S rRNA precursor. The exosome-associated helicase Mtr4 recognizes the preribosomal substrate by docking to specific sites on the 25S rRNA, captures the 3' extension of the 5.8S rRNA, and channels it toward Exo-10. The structure elucidates how the exosome forms a structural and functional unit together with its massive pre-60S substrate to process rRNA during ribosome maturation. Structure of the nuclear exosome captured on a maturing preribosome.,Schuller JM, Falk S, Fromm L, Hurt E, Conti E Science. 2018 Mar 8. pii: science.aar5428. doi: 10.1126/science.aar5428. PMID:29519915[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. Loading citation details.. Citations No citations found See AlsoReferences
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