The Yeast Ski Complex: Crystal Structure and RNA Channeling to the Exosome Complex
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The Ski complex is a conserved multiprotein assembly required for the cytoplasmic functions of the exosome, including RNA turnover, surveillance, and interference. Ski2, Ski3, and Ski8 assemble in a tetramer with 1:1:2 stoichiometry. The crystal structure of an S. cerevisiae 370 kDa core complex shows that Ski3 forms an array of 33 TPR motifs organized in N-terminal and C-terminal arms. The C-terminal arm of Ski3 and the two Ski8 subunits position the helicase core of Ski2 centrally within the complex, enhancing RNA binding. The Ski3 N-terminal arm and the Ski2 insertion domain allosterically modulate the ATPase and helicase activities of the complex. Biochemical data suggest that the Ski complex can thread RNAs directly to the exosome, coupling the helicase and the exoribonuclease through a continuous RNA channel. Finally, we identify a Ski8-binding motif common to Ski3 and Spo11, rationalizing the moonlighting properties of Ski8 in mRNA decay and meiosis.
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The model of Spo11-Ski8 resembles a previous model based on the Ski3-Ski8 complex, with Ski8 contacting a sequence in Ski3 similar to QREIF380 in Spo11, but suggests a more extensive interaction surface involving an insertion in Ski8 present in Saccharomyces species but not in Schizosaccharomyces pombe and Sordaria macrospora.
“Our model resembles a previous model based on the Ski3–Ski8 complex, with Ski8 contacting a sequence in Ski3 that is similar to the sequence QREIF380 in Spo11 (27,28) (fig. S17A), but suggests a more extensive interaction surface than previously appreciated, involving an insertion in Ski8 that is present in Saccharomyces species but not in Schizosaccharomyces pombe and Sordaria macrospora, where”
From Computed structures of core eukaryotic protein complexes (2021) · cites this paper as [28]
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- Authors
- Halbach, F., Reichelt, P., Rode, M., & Conti, E.
- Affiliations
- Max Planck Society (DE)
- Corresponding author
- Conti, Elena
- ORCID
- Conti, Elena
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2013-08
- Volume
- 154
- Issue
- 4
- Pages
- 814-826
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2046995371
- Cited by
- 210
- References
- 73
- Citations by year
- 2026: 8 · 2025: 10 · 2024: 21 · 2023: 13 · 2022: 12 · 2021: 21 · 2020: 19 · 2019: 18 · 2018: 18 · 2017: 19 · 2016: 18 · 2015: 15 · 2014: 16 · 2013: 2
- FWCI
- 7.61
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- DORA PSI (Paul Scherrer Institute) (submittedVersion)
- MPG.PuRe (Max Planck Society) (submittedVersion)
- Funders
- Boehringer Ingelheim Fonds
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA regulation and disease
- Keywords
- SKI complex, exosomes, TPR motif, crystal structure, RNA turnover, RNA surveillance, RNA interference, allosteric regulation, ATPase activity, Spo11, mRNA degradation, meiosis, Saccharomyces cerevisiae
- MeSH terms
- Amino Acid Sequence, Models, Molecular, Molecular Sequence Data, Nuclear Proteins, Saccharomyces cerevisiae, Sequence Alignment, Crystallography, X-Ray, RNA Stability, Saccharomyces cerevisiae Proteins, Exosome Multienzyme Ribonuclease Complex
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