Send to

Choose Destination
Elife. 2018 Jul 26;7. pii: e38686. doi: 10.7554/eLife.38686.

Distinct and evolutionary conserved structural features of the human nuclear exosome complex.

Author information

Department of Structural Cell Biology, Max Planck Institute of Biochemistry, Munich, Germany.
Contributed equally


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.


RNA decay; biochemistry; chemical biology; cryoEM; hDIS3; hEXO-14; hMTR4; human; molecular biophysics; nuclear exosome; structural biology

[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for eLife Sciences Publications, Ltd Icon for PubMed Central
Loading ...
Support Center