Probing Interactions between the U2 Small Nuclear Ribonucleoprotein and the DEAD-box Protein, Prp5 [PDF]
Pre-mRNA binding to the yeast U2 small nuclear ribonucleoprotein (snRNP) during prespliceosome formation requires ATP hydrolysis, the highly conserved UACUAAC box of the branch point region of the pre-mRNA, and several factors. Here we analyzed the binding of a radiolabeled 2'-O-methyl oligonucleotide complementary to U2 small nuclear RNA to study ...
Barham K Abu, Abu Dayyeh +3 more
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Identification, purification, and biochemical characterization of U2 small nuclear ribonucleoprotein auxiliary factor. [PDF]
Binding of U2 small nuclear ribonucleoprotein (snRNP) to the pre-mRNA branch site is an early step in spliceosome assembly and appears to commit a pre-mRNA to the splicing pathway. We have shown previously that this ATP-dependent binding requires a non-rnRNP factor, U2 snRNP auxiliary factor (U2AF), in addition to U2 snRNP.
P D, Zamore, M R, Green
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Malleable ribonucleoprotein machine: protein intrinsic disorder in the Saccharomyces cerevisiae spliceosome [PDF]
Recent studies revealed that a significant fraction of any given proteome is presented by proteins that do not have unique 3D structures as a whole or in significant parts.
Maria de Lourdes Coelho Ribeiro +9 more
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Identification and Characterization of a Yeast Gene Encoding the U2 Small Nuclear Ribonucleoprotein Particle B″ Protein [PDF]
The inessential yeast gene MUD2 encodes a protein factor that contributes to U1 small nuclear ribonucleoprotein particle (snRNP)-pre-mRNA complex (commitment complex) formation. To identify other genes that contribute to this early splicing step, we performed a synthetic lethal screen with a MUD2 deletion strain.
J, Tang, N, Abovich, M, Rosbash
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Hexanucleotide repeat expansion in the C9ORF72 gene results in production of dipeptide repeat (DPR) proteins that may disrupt pre-mRNA splicing in amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD) patients.
Shanye Yin +7 more
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Interaction Domains and Nuclear Targeting Signals in Subunits of the U2 Small Nuclear Ribonucleoprotein Particle-associated Splicing Factor SF3a [PDF]
Human splicing factor SF3a is a component of the mature U2 small nuclear ribonucleoprotein particle (snRNP) and its three subunits of 60, 66, and 120 kDa are essential for splicing in vitro and in vivo. The SF3a heterotrimer forms in the cytoplasm and enters the nucleus independently of the U2 snRNP. Here, we have analyzed domains required for in vitro
Huang CJ +3 more
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Assembly of the U2 small nuclear ribonucleoprotein from Trypanosoma brucei. A mutational analysis
trans-Splicing in trypanosomes requires the functions of U2 and U4/U6 small nuclear (sn) RNPs. We have analyzed protein binding and assembly of the Trypanosoma brucei U2 snRNP, using specific antibodies against U2 snRNP proteins and in vitro reconstitution assays of U2 deletion derivatives and human-trypanosome hybrid RNAs.
A, Günzl +3 more
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Recognition of U1 and U2 Small Nuclear RNAs Can Be Altered by a 5-Amino-Acid Segment in the U2 Small Nuclear Ribonucleoprotein Particle (snRNP) B″ Protein and through Interactions with U2 snRNP-A′ Protein [PDF]
We have investigated the sequence elements influencing RNA recognition in two closely related small nuclear ribonucleoprotein particle (snRNP) proteins, U1 snRNP-A and U2 snRNP-B". A 5-amino-acid segment in the RNA-binding domain of the U2 snRNP-B" protein was found to confer U2 RNA recognition when substituted into the corresponding position in the U1
R C, Bentley, J D, Keene
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Crystal Structure of Prp5p Reveals Interdomain Interactions that Impact Spliceosome Assembly
The DEAD-box adenosine triphosphatase (ATPase) Prp5p facilitates U2 small nuclear ribonucleoprotein particle (snRNP) binding to the intron branch site region during spliceosome assembly. We present crystal structures of S.
Zhi-Min Zhang +7 more
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The U1 RNA-binding site of the U1 small nuclear ribonucleoprotein (snRNP)-associated A protein suggests a similarity with U2 snRNPs. [PDF]
The site of interaction between human U1 RNA and one of its uniquely associated proteins, A, was examined with in vitro binding assays. The A protein bound directly to stem-loop II of U1 RNA in a region which exhibits sequence similarity to U2 RNA.
C, Lutz-Freyermuth +2 more
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