Results 11 to 20 of about 8,536 (192)

Ecd promotes U5 snRNP maturation and Prp8 stability. [PDF]

Nucleic Acids Res, 2021
Abstract Pre-mRNA splicing catalyzed by the spliceosome represents a critical step in the regulation of gene expression contributing to transcriptome and proteome diversity. The spliceosome consists of five small nuclear ribonucleoprotein particles (snRNPs), the biogenesis of which remains only partially understood.
Erkelenz S, Stanković D, Mundorf J, Bresser T, Claudius AK, Boehm V, Gehring NH, Uhlirova M.   +7 more
europepmc   +4 more sources

Reovirus μ2 Protein Impairs Translation to Reduce U5 snRNP Protein Levels. [PDF]

Int J Mol Sci, 2022
Mammalian orthoreovirus (MRV) is a double-stranded RNA virus from the Reoviridae family that infects a large range of mammals, including humans. Recently, studies have shown that MRV alters cellular alternative splicing (AS) during viral infection. The structural protein μ2 appears to be the main determinant of these AS modifications by decreasing the ...
Boudreault S, Martineau CA, Faucher-Giguère L, Abou-Elela S, Lemay G, Bisaillon M.   +5 more
europepmc   +3 more sources

Structure of the human 20S U5 snRNP. [PDF]

Nat Struct Mol Biol
AbstractThe 20S U5 small nuclear ribonucleoprotein particle (snRNP) is a 17-subunit RNA–protein complex and a precursor of the U4/U6.U5 tri-snRNP, the major building block of the precatalytic spliceosome. CD2BP2 is a hallmark protein of the 20S U5 snRNP, absent from the mature tri-snRNP.
Schneider S, Brandina I, Peter D, Lagad S, Fraudeau A, Portell-Montserrat J, Tholen J, Zhao J, Galej WP.   +8 more
europepmc   +4 more sources

Mechanism for Aar2p function as a U5 snRNP assembly factor. [PDF]

Genes Dev, 2011
Little is known about how particle-specific proteins are assembled on spliceosomal small nuclear ribonucleoproteins (snRNPs). Brr2p is a U5 snRNP-specific RNA helicase required for spliceosome catalytic activation and disassembly. In yeast, the Aar2 protein is part of a cytoplasmic precursor U5 snRNP that lacks Brr2p and is replaced by Brr2p in the ...
Weber G, Cristão VF, de L Alves F, Santos KF, Holton N, Rappsilber J, Beggs JD, Wahl MC.   +7 more
europepmc   +5 more sources

Structural basis of human U5 snRNP late biogenesis and recycling. [PDF]

Nat Struct Mol Biol
Pre-mRNA splicing by the spliceosome requires the biogenesis and recycling of its small nuclear ribonucleoprotein (snRNP) complexes, which are consumed in each round of splicing. The human U5 snRNP is the ~1 MDa 'heart' of the spliceosome and is recycled through an unknown mechanism involving major architectural rearrangements and the dedicated ...
Riabov Bassat D, Visanpattanasin S, Vorländer MK, Fin L, Phillips AW, Plaschka C.   +5 more
europepmc   +3 more sources

The human U5 snRNP 52K protein (CD2BP2) interacts with U5-102K (hPrp6), a U4/U6.U5 tri-snRNP bridging protein, but dissociates upon tri-snRNP formation [PDF]

RNA, 2005
The U5 snRNP plays an essential role in both U2- and U12-dependent splicing. Here, we have characterized a 52-kDa protein associated with the human U5 snRNP, designated U5-52K. Protein sequencing revealed that U5-52K is identical to the CD2BP2, which interacts with the cytoplasmic portion of the human T-cell surface protein CD2.
Laggerbauer, B., Liu, S., Makarov, E., Vornlocher, H., Makarova, O., Ingelfinger, D., Achsel, T., Luehrmann, R.   +7 more
openaire   +3 more sources

Assembly of the U5 snRNP component PRPF8 is controlled by the HSP90/R2TP chaperones. [PDF]

J Cell Biol, 2017
Splicing is catalyzed by the spliceosome, a complex of five major small nuclear ribonucleoprotein particles (snRNPs). The pre-mRNA splicing factor PRPF8 is a crucial component of the U5 snRNP, and together with EFTUD2 and SNRNP200, it forms a central module of the spliceosome.
Malinová A, Cvačková Z, Matějů D, Hořejší Z, Abéza C, Vandermoere F, Bertrand E, Bertrand E, Staněk D, Verheggen C.   +9 more
europepmc   +6 more sources

A Novel N-Terminal <i>PRPF6</i> Variant in Autosomal Dominant Retinitis Pigmentosa. [PDF]

Clin Case Rep
ABSTRACT This report identifies the first N‐terminal PRPF6 variant (c.514C>T) as a cause of autosomal dominant Retinitis Pigmentosa. This novel variant is associated with progressive peripheral vision loss but notably preserved central visual acuity, suggesting a distinct phenotypic expression compared to C‐terminal variants.
Li N, Dang Y.
europepmc   +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]

PLoS ONE, 2014
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, Anja Hirmer, Andreas Gal, Klaus Rüther, Hanno Jörn Bolz, Christoph Winkler, Bernhard Laggerbauer, Utz Fischer   +7 more
doaj   +1 more source

Role of Cajal bodies and nucleolus in the maturation of the U1 snRNP in Arabidopsis. [PDF]

PLoS ONE, 2008
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