ArticleProtein science : a publication of the Protein Society2004
The structure of Ski8p, a protein regulating mRNA degradation: Implications for WD protein structure.
Article in Protein science : a publication of the Protein Society, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 53 citations in OpenAlex.
- Article
- Mechanism and Control of Meiotic DNA Double-Strand Break Formation inFrontiers in cell and developmental biology · 2021Review
- Structural and functional characterization of the Spo11 core complex.Nature structural & molecular biology · 2021Article
- Purification and Reconstitution of the S. cerevisiae TRAMP and Ski Complexes for Biochemical and Structural Studies.Methods in molecular biology (Clifton, N.J.) · 2020Article
- The substrate specificity of eukaryotic cytosolic chaperonin CCT.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018Review
- Ski2-like RNA helicase structures: common themes and complex assemblies.RNA biology · 2013Review
- Functional interactions among members of the meiotic initiation complex in fission yeast.Current genetics · 2010Article
- The Prp19 WD40 domain contains a conserved protein interaction region essential for its function.Structure (London, England : 1993) · 2010Article
- Electrostatic and functional analysis of the seven-bladed WD beta-propellers.Evolutionary bioinformatics online · 2008Article
- Biochemistry of Meiotic Recombination: Formation, Processing, and Resolution of Recombination Intermediates.Genome dynamics and stability · 2008Article
- The yeast Ski complex is a hetero-tetramer.Protein science : a publication of the Protein Society · 2008Article
- Spo11 and the Formation of DNA Double-Strand Breaks in Meiosis.Genome dynamics and stability · 2008Article
- Partner proteins that interact with Clonorchis sinensis WD40-repeat protein.Parasitology research · 2007Article
- Three-dimensional structures of the flagellar dynein-microtubule complex by cryoelectron microscopy.The Journal of cell biology · 2007Article
- A new Drosophila gene wh (wuho) with WD40 repeats is essential for spermatogenesis and has maximal expression in hub cells.Developmental biology · 2006Article
- Protein structure database search and evolutionary classification.Nucleic acids research · 2006Article
- Bioinformatic analyses implicate the collaborating meiotic crossover/chiasma proteins Zip2, Zip3, and Spo22/Zip4 in ubiquitin labeling.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
- Ge-1 is a central component of the mammalian cytoplasmic mRNA processing body.RNA (New York, N.Y.) · 2005Article
- TANMEI/EMB2757 encodes a WD repeat protein required for embryo development in Arabidopsis.Plant physiology · 2005Article
- Domain interactions within the Ski2/3/8 complex and between the Ski complex and Ski7p.RNA (New York, N.Y.) · 2005Article
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2 authors at 1 institution in 1 country.
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Abstract
Ski8p is a 44-kD protein that primarily functions in the regulation of exosome-mediated, 3'--> 5' degradation of damaged mRNA. It does so by forming a complex with two partner proteins, Ski2p and Ski3p, which complete a complex that is capable of recruiting and activating the exosome/Ski7p complex that functions in RNA degradation. Ski8p also functions in meiotic recombination in complex with Spo11 in yeast. It is one of the many hundreds of primarily eukaryotic proteins containing tandem copies of WD repeats (also known as WD40 or beta-transducin repeats), which are short ~40 amino acid motifs, often terminating in a Trp-Asp dipeptide. Genomic analyses have demonstrated that WD repeats are found in 1%-2% of proteins in a typical eukaryote, but are extremely rare in prokaryotes. Almost all structurally characterized WD-repeat proteins are composed of seven such repeats and fold into seven-bladed beta propellers. Ski8p was thought to contain five WD repeats on the basis of primary sequence analysis implying a five-bladed propeller. The 1.9 A crystal structure unexpectedly exhibits a seven-bladed propeller fold with seven structurally authentic WD repeats. Structure-based sequence alignments show additional sequence diversity in the two undetected repeats. This demonstrates that many WD repeats have not yet been identified in sequences and also raises the possibility that the seven-bladed propeller may be the predominant fold for this family of proteins.
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