Results 21 to 30 of about 12,575 (173)
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.
A. Newman
semanticscholar +3 more sources
Assembly of Snu114 into U5 snRNP requires Prp8 and a functional GTPase domain. [PDF]
Snu114 is a U5 snRNP protein essential for pre-mRNA splicing. Based on its homology with the ribosomal translocase EF-G, it is thought that GTP hydrolysis by Snu114 induces conformational rearrangements in the spliceosome. We recently identified allele-specific genetic interactions between SNU114 and genes encoding three other U5 snRNP components, Prp8
T. Brenner, C. Guthrie
semanticscholar +3 more sources
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.
T. Nielsen +3 more
semanticscholar +5 more sources
The Dengue Virus NS5 Protein Intrudes in the Cellular Spliceosome and Modulates Splicing. [PDF]
Dengue virus NS5 protein plays multiple functions in the cytoplasm of infected cells, enabling viral RNA replication and counteracting host antiviral responses. Here, we demonstrate a novel function of NS5 in the nucleus where it interferes with cellular
Federico A De Maio +12 more
doaj +1 more source
In yeast, TFIP11 and DHX15 promote the disassembly of spliceosome complex after splicing is completed. Here the authors show that human TFIP11 functions independently of DHX15 and is required for U6 snRNA 2’-O-methylation and U4/U6.U5 tri-snRNP assembly.
Amandine Duchemin +14 more
doaj +1 more source
The architecture of the spliceosomal U4/U6.U5 tri-snRNP [PDF]
U4/U6.U5 tri-snRNP is a 1.5-megadalton pre-assembled spliceosomal complex comprising U5 small nuclear RNA (snRNA), extensively base-paired U4/U6 snRNAs and more than 30 proteins, including the key components Prp8, Brr2 and Snu114. The tri-snRNP combines with a precursor messenger RNA substrate bound to U1 and U2 small nuclear ribonucleoprotein ...
Nguyen, Thi Hoang Duong +6 more
openaire +2 more sources
Identification of a PRPF4 loss-of-function variant that abrogates U4/U6.U5 tri-snRNP integration and is associated with retinitis pigmentosa. [PDF]
Pre-mRNA splicing by the spliceosome is an essential step in the maturation of nearly all human mRNAs. Mutations in six spliceosomal proteins, PRPF3, PRPF4, PRPF6, PRPF8, PRPF31 and SNRNP200, cause retinitis pigmentosa (RP), a disease characterized by ...
Bastian Linder +7 more
doaj +1 more source
The recruitment of the U5 snRNP to nascent transcripts requires internal loop 1 of U5 snRNA [PDF]
In this study, we take advantage of the high spatial resolution offered by the nucleus and lampbrush chromosomes of the amphibian oocyte to investigate the mechanisms that regulate the intranuclear trafficking of the U5 snRNP and its recruitment to nascent transcripts.
Rebecca, Kim +3 more
openaire +2 more sources
Role of Cajal bodies and nucleolus in the maturation of the U1 snRNP in Arabidopsis. [PDF]
BACKGROUND: The biogenesis of spliceosomal snRNPs takes place in both the cytoplasm where Sm core proteins are added and snRNAs are modified at the 5' and 3' termini and in the nucleus where snRNP-specific proteins associate.
Zdravko J Lorković, Andrea Barta
doaj +1 more source
Summary: The spliceosome is a large ribonucleoprotein complex responsible for pre-mRNA splicing and genome stability maintenance. Disruption of the spliceosome activity may lead to developmental disorders and tumorigenesis.
Gui-Xin Ruan +8 more
doaj +1 more source

