ArticleRNA (New York, N.Y.)1998
Conservation of structure and subunit interactions in yeast homologues of splicing factor 3b (SF3b) subunits.
Article in RNA (New York, N.Y.), 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 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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Who cites it
32 citing papers in PubMed, 50 citations in OpenAlex.
- JANUS, a spliceosome-associated protein, promotes miRNA biogenesis in Arabidopsis.Nucleic acids research · 2024Article
- Sequence Divergence and Functional Specializations of the Ancient Spliceosomal SF3b: Implications in Flexibility and Adaptations of the Multi-Protein Complex.Frontiers in genetics · 2021Article
- SF3b4: A Versatile Player in Eukaryotic Cells.Frontiers in cell and developmental biology · 2020Review
- Arabidopsis JANUS Regulates Embryonic Pattern Formation through Pol II-Mediated Transcription of WOX2 and PIN7.iScience · 2019Article
- Component of splicing factor SF3b plays a key role in translational control of polyribosomes on the endoplasmic reticulum.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- An RNA Recognition Motif-Containing Protein Functions in Meiotic Silencing by Unpaired DNA.G3 (Bethesda, Md.) · 2017Article
- Structure of a pre-catalytic spliceosome.Nature · 2017Article
- Crystal structure of U2 snRNP SF3b components: Hsh49p in complex with Cus1p-binding domain.RNA (New York, N.Y.) · 2017Article
- Solution structure of the first RNA recognition motif domain of human spliceosomal protein SF3b49 and its mode of interaction with a SF3b145 fragment.Protein science : a publication of the Protein Society · 2017Article
- A unique spatial arrangement of the snRNPs within the native spliceosome emerges from in silico studies.Structure (London, England : 1993) · 2012Article
- An investigation of a role for U2 snRNP spliceosomal components in regulating transcription.PloS one · 2011Article
- DExD/H-box Prp5 protein is in the spliceosome during most of the splicing cycle.RNA (New York, N.Y.) · 2009Article
- Telomerase-associated protein 1, HSP90, and topoisomerase IIalpha associate directly with the BLM helicase in immortalized cells using ALT and modulate its helicase activity using telomeric DNA substrates.The Journal of biological chemistry · 2009Article
- Human immunodeficiency virus type 1 Vpr induces G2 checkpoint activation by interacting with the splicing factor SAP145.Molecular and cellular biology · 2006Article
- U2 snRNA-protein contacts in purified human 17S U2 snRNPs and in spliceosomal A and B complexes.Molecular and cellular biology · 2006Article
- Interactions of the yeast SF3b splicing factor.Molecular and cellular biology · 2005Article
- Novel DNA-binding properties of the RNA-binding protein TIAR.Nucleic acids research · 2005Article
- A family of RS domain proteins with novel subcellular localization and trafficking.Nucleic acids research · 2005Article
- Proteomic analysis identifies a new complex required for nuclear pre-mRNA retention and splicing.The EMBO journal · 2004Article
- Mer1p is a modular splicing factor whose function depends on the conserved U2 snRNP protein Snu17p.Nucleic acids research · 2004Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Human SAP 49, a subunit of the multimeric splicing factor 3b (SF3b), contains two RNA recognition motifs (RRMs) and binds another SF3b subunit called SAP 145, whose yeast homologue is CUS1. Here we show that the predicted yeast open reading frame YOR319w (HSH49) encodes an essential yeast splicing factor. Using bacterially expressed proteins, we find that yeast HSH49 binds CUS1. Mutations that alter putative RNA-binding residues of either HSH49 RRM are lethal in vivo, but do not prevent binding to CUS1 in vitro, suggesting that the predicted RNA-binding surfaces of HSH49 are not required for interaction with CUS1. In vivo interaction tests show that HSH49 and CUS1 associate primarily through the N-terminal RRM of HSH49. Recombinant HSH49 protein has a general RNA-binding activity that does not require CUS1. The parallels in structure and interaction between two SF3b subunits from yeast implies that the mechanism of SF3b action is highly conserved.
Indexed as
Identifiers
9436903PMC1369591W2166992176What OpenQuestion holds
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.