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SAP30BP interacts with RBM17/SPF45 to promote splicing in a subset of human short introns.
Cell Rep., DOI: 10.1016/j.celrep.2023.113534:113534 (2023)
Human pre-mRNA splicing requires the removal of introns with highly variable lengths, from tens to over a million nucleotides. Therefore, mechanisms of intron recognition and splicing are likely not universal. Recently, we reported that splicing in a subset of human short introns with truncated polypyrimidine tracts depends on RBM17 (SPF45), instead of the canonical splicing factor U2 auxiliary factor (U2AF) heterodimer. Here, we demonstrate that SAP30BP, a factor previously implicated in transcriptional control, is an essential splicing cofactor for RBM17. In vitro binding and nuclear magnetic resonance analyses demonstrate that a U2AF-homology motif (UHM) in RBM17 binds directly to a newly identified UHM-ligand motif in SAP30BP. We show that this RBM17-SAP30BP interaction is required to specifically recruit RBM17 to phosphorylated SF3B1 (SF3b155), a U2 small nuclear ribonucleoprotein (U2 snRNP) component in active spliceosomes. We propose a mechanism for splicing in a subset of short introns, in which SAP30BP guides RBM17 in the assembly of active spliceosomes.
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Publication type
Article: Journal article
Document type
Scientific Article
Keywords
Cp: Molecular Biology ; Rbm17 ; Sab30bp ; Sf3b1 ; Sf3b155 ; Spf45 ; U2 Snrnp ; U2af Heterodimer ; U2af-homology Motif ; Uhm ; Uhm-ligand Motif ; Ulm ; Polypyrimidine Tract ; Pre-mrna Splicing ; Short Intron
ISSN (print) / ISBN
2211-1247
e-ISSN
2211-1247
Journal
Cell Reports
Quellenangaben
Article Number: 113534
Publisher
Cell Press
Non-patent literature
Publications
Reviewing status
Peer reviewed
Institute(s)
Institute of Structural Biology (STB)