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

Gerlach, Piotr; Schuller, Jan M.; Bonneau, Fabien; Basquin, Jerome; Reichelt, Peter; Falk, Sebastian; Conti, Elena

doi:10.7554/eLife.38686

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

MPS-Authors

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Gerlach, Piotr
Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society;

/persons/resource/persons98592

Schuller, Jan M.
Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society;

/persons/resource/persons77784

Bonneau, Fabien
Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society;

/persons/resource/persons77713

Basquin, Jerome
Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society;

/persons/resource/persons78554

Reichelt, Peter
Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society;

/persons/resource/persons131138

Falk, Sebastian
Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society;

/persons/resource/persons77867

Conti, Elena
Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society;

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elife-38686-v2.pdf
(出版社版), 12MB

付随資料 (公開)

elife-38686-figures-v2.pdf
(付録資料), 24MB

引用

Gerlach, P., Schuller, J. M., Bonneau, F., Basquin, J., Reichelt, P., Falk, S., & Conti, E. (2018). Distinct and evolutionary conserved structural features of the human nuclear exosome complex. eLife, 7:. doi:10.7554/eLife.38686.

引用: https://hdl.handle.net/21.11116/0000-0001-F933-D

要旨

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 angstrom 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.