3SBG
Crystal structure of a Prp8 C-terminal fragment
Summary for 3SBG
| Entry DOI | 10.2210/pdb3sbg/pdb |
| Related | 3SBS 3SBT |
| Descriptor | Pre-mRNA-splicing factor 8 (1 entity in total) |
| Functional Keywords | prp8p, rnaseh domain, jab1/mpn domain, splicing |
| Biological source | Saccharomyces cerevisiae (Baker's yeast) |
| Cellular location | Nucleus: P33334 |
| Total number of polymer chains | 1 |
| Total formula weight | 64029.83 |
| Authors | Weber, G.,Santos, K.,Holton, N.,Wahl, M.C. (deposition date: 2011-06-04, release date: 2012-04-18, Last modification date: 2024-02-28) |
| Primary citation | Weber, G.,Cristao, V.F.,de L Alves, F.,Santos, K.F.,Holton, N.,Rappsilber, J.,Beggs, J.D.,Wahl, M.C. Mechanism for Aar2p function as a U5 snRNP assembly factor. Genes Dev., 25:1601-1612, 2011 Cited by PubMed Abstract: 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 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. PubMed: 21764848DOI: 10.1101/gad.635911 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.28 Å) |
Structure validation
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