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TitleDistinct and evolutionary conserved structural features of the human nuclear exosome complex.
Journal, issue, pagesElife, Vol. 7, Year 2018
Publish dateJul 26, 2018
AuthorsPiotr Gerlach / Jan M Schuller / Fabien Bonneau / Jérôme Basquin / Peter Reichelt / Sebastian Falk / Elena Conti /
PubMed AbstractThe nuclear RNA exosome complex mediates the processing of structured RNAs and the decay of aberrant non-coding RNAs, an important function particularly in human cells. Most mechanistic studies to ...The nuclear RNA exosome complex mediates the processing of structured RNAs and the decay of aberrant non-coding RNAs, an important function particularly in human cells. Most mechanistic studies to date have focused on the yeast system. Here, we reconstituted and studied the properties of a recombinant 14-subunit human nuclear exosome complex. In biochemical assays, the human exosome embeds a longer RNA channel than its yeast counterpart. The 3.8 Å resolution cryo-EM structure of the core complex bound to a single-stranded RNA reveals that the RNA channel path is formed by two distinct features of the hDIS3 exoribonuclease: an open conformation and a domain organization more similar to bacterial RNase II than to yeast Rrp44. The cryo-EM structure of the holo-complex shows how obligate nuclear cofactors position the hMTR4 helicase at the entrance of the core complex, suggesting a striking structural conservation from lower to higher eukaryotes.
External linksElife / PubMed:30047866 / PubMed Central
MethodsEM (single particle)
Resolution3.8 - 6.25 Å
Structure data

EMDB-0127:
Human nuclear RNA exosome EXO-14 complex
Method: EM (single particle) / Resolution: 6.25 Å

0128

6h25

EMDB-0128, PDB-6h25:
Human nuclear RNA exosome EXO-10-MPP6 complex
Method: EM (single particle) / Resolution: 3.8 Å

Source
  • synthetic construct (others)
  • homo sapiens (human)
KeywordsRNA BINDING PROTEIN / nuclear exosome / RNA decay / cryoEM / hEXO-10 / hDIS3 / hMPP6

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