The structure of the ASAP core complex reveals the existence of a Pinin-containing PSAP complex.
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-A 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.
Mesh Terms:
Amino Acid Motifs, Amino Acid Sequence, Animals, Carrier Proteins, Cell Adhesion Molecules, Cell Line, Crystallography, X-Ray, Drosophila Proteins, Drosophila melanogaster, Histone Deacetylases, Humans, Mice, Microtubule-Associated Proteins, Molecular Sequence Data, Nuclear Proteins, Protein Binding, Ribonucleoproteins, Saposins, Sequence Alignment, Transcription Factors
Amino Acid Motifs, Amino Acid Sequence, Animals, Carrier Proteins, Cell Adhesion Molecules, Cell Line, Crystallography, X-Ray, Drosophila Proteins, Drosophila melanogaster, Histone Deacetylases, Humans, Mice, Microtubule-Associated Proteins, Molecular Sequence Data, Nuclear Proteins, Protein Binding, Ribonucleoproteins, Saposins, Sequence Alignment, Transcription Factors
Nat. Struct. Mol. Biol.
Date: Apr. 01, 2012
PubMed ID: 22388736
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