4A8X

Structure of the core ASAP complex

Summary for 4A8X

• Entry DOI: 10.2210/pdb4a8x/pdb
• Related: 4A6Q 4A90
• Descriptor: RNA-BINDING PROTEIN WITH SERINE-RICH DOMAIN 1, HOOK-LIKE, ISOFORM A, HISTONE DEACETYLASE COMPLEX SUBUNIT SAP18, ... (4 entities in total)
• Functional Keywords: transcription, splicing, rna processing, nonsense mediated decay, nmd, hdac, histone deacetylation
• Biological source: HOMO SAPIENS; More
• Cellular location: Nucleus: Q15287; Nucleus (By similarity): O55128
• Total number of polymer chains: 3
• Total formula weight: 29747.25

Authors

Murachelli, A.G.,Ebert, J.,Basquin, C.,Le Hir, H.,Conti, E. (deposition date: 2011-11-21, release date: 2012-03-07, Last modification date: 2023-12-20)

Primary citation

Murachelli, A.G.,Ebert, J.,Basquin, C.,Le Hir, H.,Conti, E.
The Structure of the Asap Core Complex Reveals the Existence of a Pinin-Containing Psap Complex
Nat.Struct.Mol.Biol., 19:378-, 2012

PubMed Abstract: The ASAP complex interacts with the exon-junction complex (EJC), a messenger ribonucleoprotein complex involved in post-transcriptional regulation. The three ASAP subunits (Acinus, RNPS1 and SAP18) have been individually implicated in transcriptional regulation, pre-mRNA splicing and mRNA quality control. To shed light on the basis for and consequences of ASAP's interaction with the EJC, we have determined the 1.9-Å resolution structure of a eukaryotic ASAP core complex. The RNA-recognition motif of RNPS1 binds to a conserved motif of Acinus with a recognition mode similar to that observed in splicing U2AF proteins. The Acinus-RNPS1 platform recruits the ubiquitin-like domain of SAP18, forming a ternary complex that has both RNA- and protein-binding properties. Unexpectedly, our structural analysis identified an Acinus-like motif in Pinin, another EJC-associated splicing factor. We show that Pinin physically interacts with RNPS1 and SAP18, forming an alternative ternary complex, PSAP.

PubMed: 22388736
DOI: 10.1038/NSMB.2242

Experimental method

X-RAY DIFFRACTION (1.9 Å)