3sbt: Difference between revisions
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3sbt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sbt OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3sbt RCSB], [http://www.ebi.ac.uk/pdbsum/3sbt PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3sbt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sbt OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3sbt RCSB], [http://www.ebi.ac.uk/pdbsum/3sbt PDBsum]</span></td></tr> | ||
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== Function == | |||
[[http://www.uniprot.org/uniprot/PRP8_YEAST PRP8_YEAST]] Required for pre-spliceosome formation, which is the first step of pre-mRNA splicing. This protein is associated with snRNP U5. Has a role in branch site-3' splice site selection. Associates with the branch site-3' splice 3'-exon region. Also has a role in cell cycle.<ref>PMID:2835658</ref> <ref>PMID:9150140</ref> <ref>PMID:12773561</ref> <ref>PMID:18779563</ref> [[http://www.uniprot.org/uniprot/AAR2_YEAST AAR2_YEAST]] Involved in splicing pre-mRNA of the A1 cistron and other genes that are important for cell growth. | |||
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== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Revision as of 20:34, 25 December 2014
Crystal structure of a Aar2-Prp8 complexCrystal structure of a Aar2-Prp8 complex
Structural highlights
Function[PRP8_YEAST] Required for pre-spliceosome formation, which is the first step of pre-mRNA splicing. This protein is associated with snRNP U5. Has a role in branch site-3' splice site selection. Associates with the branch site-3' splice 3'-exon region. Also has a role in cell cycle.[1] [2] [3] [4] [AAR2_YEAST] Involved in splicing pre-mRNA of the A1 cistron and other genes that are important for cell growth. Publication Abstract from PubMedLittle 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 nucleus. Here we show that Aar2p and Brr2p bind to different domains in the C-terminal region of Prp8p; Aar2p interacts with the RNaseH domain, whereas Brr2p interacts with the Jab1/MPN domain. These domains are connected by a long, flexible linker, but the Aar2p-RNaseH complex sequesters the Jab1/MPN domain, thereby preventing binding by Brr2p. Aar2p is phosphorylated in vivo, and a phospho-mimetic S253E mutation in Aar2p leads to disruption of the Aar2p-Prp8p complex in favor of the Brr2p-Prp8p complex. We propose a model in which Aar2p acts as a phosphorylation-controlled U5 snRNP assembly factor that regulates the incorporation of the particle-specific Brr2p. The purpose of this regulation may be to safeguard against nonspecific RNA binding to Prp8p and/or premature activation of Brr2p activity. Mechanism for Aar2p function as a U5 snRNP assembly factor.,Weber G, Cristao VF, Alves FD, Santos KF, Holton N, Rappsilber J, Beggs JD, Wahl MC Genes Dev. 2011 Jul 15. PMID:21764848[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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