Structural basis of human U5 snRNP late biogenesis and recycling. [PDF]
Nat Struct Mol BiolPre-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
Riabov Bassat D +5 more
europepmc +4 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 ...
Malinová A +9 more
europepmc +7 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.
Weber G +7 more
europepmc +6 more sources
Structural basis for dual roles of Aar2p in U5 snRNP assembly. [PDF]
Genes Dev, 2013 Yeast U5 small nuclear ribonucleoprotein particle (snRNP) is assembled via a cytoplasmic precursor that contains the U5-specific Prp8 protein but lacks the U5-specific Brr2 helicase.
Weber G +8 more
europepmc +7 more sources
An unanticipated early function of DEAD-box ATPase Prp28 during commitment to splicing is modulated by U5 snRNP protein Prp8. [PDF]
RNA, 2014 Prp28 is a “DEAD-box” ATPase that promotes displacement of the U1 snRNP from the intron 5′ splice site during spliceosome activation. This study shows that Prp28 has an unexpected, earlier, ATP-independent function in splicing complex formation.
Price AM +3 more
europepmc +2 more sources
Structure, 2013 Summary The U5 small nuclear ribonucleoprotein particle (snRNP) helicase Brr2 disrupts the U4/U6 small nuclear RNA (snRNA) duplex and allows U6 snRNA to engage in an intricate RNA network at the active center of the spliceosome.
Nguyen TH +5 more
europepmc +2 more sources
The U5 snRNA internal loop 1 is a platform for Brr2, Snu114 and Prp8 protein binding during U5 snRNP assembly. [PDF]
J Cell Biochem, 2013 The U5 small nuclear ribonucleoprotein particle (snRNP) forms the heart of the spliceosome which is required for intron removal from pre‐mRNA. The proteins Prp8, Snu114 and Brr2 all assemble with the U5 small nuclear RNA (snRNA) to produce the U5 snRNP ...
Nancollis V +3 more
europepmc +2 more sources
A novel role for a U5 snRNP protein in 3' splice site selection. [PDF]
Genes & Development, 1995 The choice of a 3' splice site in Saccharomyces cerevisiae introns involves recognition of a uridine-rich tract upstream of the AG dinucleotide splice junction.
J. Umen, C. Guthrie
semanticscholar +3 more sources
Protein-RNA interactions in the U5 snRNP of Saccharomyces cerevisiae.
RNA, 1998 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.
I. Dix +4 more
semanticscholar +8 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.
B. Laggerbauer +7 more
semanticscholar +4 more sources