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Journal Article

Structure of a Cytoplasmic 11-Subunit RNA Exosome Complex

MPS-Authors
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Kowalinski,  Eva
Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society;

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

/persons/resource/persons77921

Ebert,  Judith
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/persons39085

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

/persons/resource/persons101406

Habermann,  Bianca
Habermann, Bianca / Computational 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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Fulltext (public)

1-s2.0-S1097276516301915-main.pdf
(Publisher version), 4MB

Supplementary Material (public)

mmc1.pdf
(Supplementary material), 9MB

mmc2.pdf
(Supplementary material), 13MB

Citation

Kowalinski, E., Kögel, A., Ebert, J., Reichelt, P., Stegmann, E., Habermann, B., et al. (2016). Structure of a Cytoplasmic 11-Subunit RNA Exosome Complex. Molecular Cell, 63(1), 125-134. doi:10.1016/j.molcel.2016.05.028.


Cite as: http://hdl.handle.net/11858/00-001M-0000-002B-9DAE-C
Abstract
The RNA exosome complex associates with nuclear and cytoplasmic cofactors to mediate the decay, surveillance, or processing of a wide variety of transcripts. In the cytoplasm, the conserved core of the exosome (Exo10) functions together with the conserved Ski complex. The interaction of S. cerevisiae Exo10 and Ski is not direct but requires a bridging cofactor, Ski7. Here, we report the 2.65 angstrom resolution structure of S. cerevisiae Exo10 bound to the interacting domain of Ski7. Extensive hydrophobic interactions rationalize the high affinity and stability of this complex, pointing to Ski7 as a constitutive component of the cytosolic exosome. Despite the absence of sequence homology, cytoplasmic Ski7 and nuclear Rrp6 bind Exo(10) using similar surfaces and recognition motifs. Knowledge of the interacting residues in the yeast complexes allowed us to identify a splice variant of human HBS1-Like as a Ski7-like exosome-binding protein, revealing the evolutionary conservation of this cytoplasmic cofactor.