ArticleStructure (London, England : 1993)2015
Saccharomyces cerevisiae Ski7 Is a GTP-Binding Protein Adopting the Characteristic Conformation of Active Translational GTPases.
Article in Structure (London, England : 1993), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
20 citing papers in PubMed, 33 citations in OpenAlex.
- Genetic dissection reveals distinct contributions of the eS31 N-terminal domain to translational accuracy in Saccharomyces cerevisiae.The FEBS journal · 2026Article
- The ribosome as a platform to coordinate mRNA decay.Nucleic acids research · 2025Review
- The Beak of Eukaryotic Ribosomes: Life, Work and Miracles.Biomolecules · 2024Review
- Concerted structural rearrangements enable RNA channeling into the cytoplasmic Ski238-Ski7-exosome assembly.Molecular cell · 2023Article
- Catalytic activities, molecular connections, and biological functions of plant RNA exosome complexes.The Plant cell · 2022Review
- RNA helicases are hubs that orchestrate exosome-dependent 3'-5' decay.Current opinion in structural biology · 2021Review
- Zebrafish Ski7 tunes RNA levels during the oocyte-to-embryo transition.PLoS genetics · 2021Article
- In Vitro Characterization of the Activity of the Mammalian RNA Exosome on mRNAs in Ribosomal Translation Complexes.Methods in molecular biology (Clifton, N.J.) · 2020Article
- RST1 and RIPR connect the cytosolic RNA exosome to the Ski complex in Arabidopsis.Nature communications · 2019Article
- Functions of unconventional mammalian translational GTPases GTPBP1 and GTPBP2.Genes & development · 2018Article
- Conservation of mRNA quality control factor Ski7 and its diversification through changes in alternative splicing and gene duplication.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- The nonstop decay and the RNA silencing systems operate cooperatively in plants.Nucleic acids research · 2018Article
- The Interplay between the RNA Decay and Translation Machinery in Eukaryotes.Cold Spring Harbor perspectives in biology · 2018Review
- RNA Degradation in Neurodegenerative Disease.Advances in neurobiology · 2018Review
- Metal Fluorides: Tools for Structural and Computational Analysis of Phosphoryl Transfer Enzymes.Topics in current chemistry (Cham) · 2017Review
- A short splicing isoform of HBS1L links the cytoplasmic exosome and SKI complexes in humans.Nucleic acids research · 2017Article
- Targeting RNA for processing or destruction by the eukaryotic RNA exosome and its cofactors.Genes & development · 2017Review
- Structure of a Cytoplasmic 11-Subunit RNA Exosome Complex.Molecular cell · 2016Article
- Mutations in the G-domain of Ski7 cause specific dysfunction in non-stop decay.Scientific reports · 2016Article
- CryoEM structure of yeast cytoplasmic exosome complex.Cell research · 2016Article
Corrections and comments
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Authors and funding
4 authors at 4 institutions in 2 countries.
Funding
Abstract
Ski7 is a cofactor of the cytoplasmic exosome in budding yeast, functioning in both mRNA turnover and non-stop decay (NSD), a surveillance pathway that degrades faulty mRNAs lacking a stop codon. The C-terminal region of Ski7 (Ski7C) shares overall sequence similarity with the translational GTPase (trGTPase) Hbs1, but whether Ski7 has retained the properties of a trGTPase is unclear. Here, we report the high-resolution structures of Ski7C bound to either intact guanosine triphosphate (GTP) or guanosine diphosphate-Pi. The individual domains of Ski7C adopt the conformation characteristic of active trGTPases. Furthermore, the nucleotide-binding site of Ski7C shares similar features compared with active trGTPases, notably the presence of a characteristic monovalent cation. However, a suboptimal polar residue at the putative catalytic site and an unusual polar residue that interacts with the γ-phosphate of GTP distinguish Ski7 from other trGTPases, suggesting it might function rather as a GTP-binding protein than as a GTP-hydrolyzing enzyme.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.