Structural analysis of 3' splice site recognition by U2AF/SF1 during early spliceosome assembly
In metazoan organisms, the proteome diversity is greatly expanded by alternative splicing of pre-mRNA. In the early steps of spliceosome assembly, the exon and intron boundaries need to be carefully selected, facilitated by RNA binding proteins that recognize conserved cis-regulatory sequences in the pre-mRNA. These include the branch point site recognised by SF1, followed by the poly-pyrimidine tract (PY-tract) and the 3¿ splice site (3¿-SS), which are recognised by the U2 auxiliary factor (U2AF) heterodimer. Additional UHM/ULM interactions stabilize the ternary complex of SF1 and the U2AF heterodimer. Details about the overall architecture of the human 3¿-SS recognition complex are yet to be unveiled, which is the major goal of our project. For this purpose, we recently reconstituted in vitro the ternary 3¿-SS recognition complex, composed of recombinant SF1, U2AF2 and U2AF1 proteins and the 3¿ SS RNA. By NMR spectroscopy and SAXS we could show that the protein-RNA complex is stable and functional. Studying this complex by SANS would enable us to obtain individual data of the proteins/RNA and would allow structural characterization in combination with our SAXS and NMR studies.
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The recommended format for citing this dataset in a research publication is in the following format:
MORGUET Clara; Matthias J. Brandl; GABEL Frank; MARTEL Anne; MARTINEZ LUMBRERAS Santiago and SATTLER Michael. (2023). Structural analysis of 3' splice site recognition by U2AF/SF1 during early spliceosome assembly. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-03-1062
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