Organization of Core Spliceosomal Components U5 snRNA Loop I and U4/U6 Di-snRNP within U4/U6.U5 Tri-snRNP as Revealed by Electron Cryomicroscopy [PDF]
In eukaryotes, pre-mRNA exons are interrupted by large noncoding introns. Alternative selection of exons and nucleotide-exact removal of introns are performed by the spliceosome, a highly dynamic macromolecular machine. U4/U6.U5 tri-snRNP is the largest and most conserved building block of the spliceosome.
Sander, Bjoern +6 more
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SSB-1 of the yeast Saccharomyces cerevisiae is a nucleolar-specific, silver-binding protein that is associated with the snR10 and snR11 small nuclear RNAs [PDF]
SSB-1, the yeast single-strand RNA-binding protein, is demonstrated to be a yeast nucleolar-specific, silver-binding protein. In double-label immunofluorescence microscopy experiments antibodies to two other nucleolar proteins, RNA Pol I 190-kD and ...
Abelson, John +3 more
core +2 more sources
Anti-U5 Small Nuclear Ribonucleoprotein (snRNP) Antibodies: A Rare Anti-U snRNP Specificity
We surveyed for autoantibodies to the U small nuclear ribonucleoproteins (snRNPs) in sera from 1171 patients with various connective tissue diseases by immunoprecipitation assay. We found serum, termed LaJ, which principally recognized the U5 snRNP from one patient with systemic sclerosis-polymyositis overlap syndrome. Anti-LaJ serum immunoprecipitated
Y, Okano +9 more
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A splicing-dependent transcriptional checkpoint associated with prespliceosome formation [PDF]
There is good evidence for functional interactions between splicing and transcription in eukaryotes, but how and why these processes are coupled remain unknown.
Ahn +62 more
core +1 more source
The role of U5 snRNP in pre-mRNA splicing [PDF]
The current model for the function of the U5 small nuclear ribonucleoprotein particle (snRNP) in the spliceosome proposes that U5 carries binding sites for the 5' and 3' exons, allowing the spliceosome to 'tether' the 5' exon intermediate produced by the first catalytic step and align it with the 3' exon for the second step.
openaire +2 more sources
Identification of an RNA-Dependent ATPase Activity in Mammalian U5 snRNPs [PDF]
Nuclear pre-mRNA splicing requires ATP at several steps from spliceosome assembly to product release. Here, we demonstrate that an integral component of the 20S U5 snRNP is an RNA-dependent ATPase. The ATPase activity of 20S U5 and 25S [U4/U6.U5] snRNPs purified by glycerol gradient centrifugation is strongly stimulated by homopolymeric RNA but not ...
B, Laggerbauer, J, Lauber, R, Lührmann
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Protein-RNA interactions in the U5 snRNP of Saccharomyces cerevisiae
We present here the first insights into the organization of proteins on the RNA in the U5 snRNP of Saccharomyces cerevisiae. Photo-crosslinking with uniformly labeled U5 RNA in snRNPs reconstituted in vitro revealed five contacting proteins, Prp8p, Snu114p, p30, p16, and p10, contact by the three smaller proteins requiring an intact Sm site.
Dix, I. +4 more
openaire +6 more sources
A human protein required for the second step of pre-mRNA splicing is functionally related to a yeast splicing factor [PDF]
We have identified a human splicing factor required for the second step of pre-mRNA splicing. This new protein, hPrp18, is 30% identical to the yeast splicing factor Prp18.
Horowitz, D. S., Krainer, A. R.
core +1 more source
Structural Basis for the Bifunctionality of the U5 snRNP 52K Protein (CD2BP2) [PDF]
The bifunctional protein U5-52K is associated with the spliceosomal 20 S U5 snRNP, and it also plays a role in immune response as CD2 receptor binding protein 2 (CD2BP2). U5-52K binds to the CD2 receptor via its GYF-domain specifically recognizing a proline-rich motif on the cytoplasmic surface of the receptor.
Nielsen, T. +3 more
openaire +4 more sources
Single molecule analysis reveals reversible and irreversible steps during spliceosome activation
The spliceosome is a complex machine composed of small nuclear ribonucleoproteins (snRNPs) and accessory proteins that excises introns from pre-mRNAs.
Aaron A Hoskins +4 more
doaj +1 more source

