Disease relevance of U2af50

• We developed a novel Escherichia coli copurification assay to map the domain on the Drosophila U2AF large subunit (dU2AF50) that interacts with the Drosophila small subunit (dU2AF38) [1].

High impact information on U2af50

• The protein Sex-lethal antagonizes the splicing factor U2AF to regulate alternative splicing of transformer pre-mRNA [2].
• The dU2AF50 protein is closely related to its mammalian counterpart and contains three carboxyl-terminal ribonucleoprotein consensus sequence RNA binding domains and an amino-terminal arginine- and serine-rich (R/S) domain [3].
• In sharp contrast to its essential role in U2 snRNP recruitment in vitro, the RS domain on the Drosophila large subunit homolog (dU2AF50) was completely dispensable in vivo [4].
• These results reveal an unexpected role for the splicing factor dU2AF50 in the nuclear export of intronless mRNAs [5].
• The RS domain of dU2AF50 functioned efficiently, while that of the dSRp55 protein did not [6].

Biological context of U2af50

• Sex-lethal splicing autoregulation in vivo: interactions between SEX-LETHAL, the U1 snRNP and U2AF underlie male exon skipping [7].
• In vertebrates, the binding site for U2AF is the pyrimidine tract located between the branch point and 3' splice site [8].
• We suggest that U2AF- and/or SRp54-mediated intron bridging may be an alternative early recognition mode to SF1-directed bridging for small introns, suggesting gene-specific early spliceosome assembly [8].
• Distinct factor requirements for exonic splicing enhancer function and binding of U2AF to the polypyrimidine tract [9].

Associations of U2af50 with chemical compounds

• When the Drosophila small-subunit homolog (dU2AF38) was complexed with the large-subunit (dU2AF50) pyrimidine tract, RNA binding activity increased 20-fold over that of free dU2AF50 [10].

Physical interactions of U2af50

• We have previously shown that SXL blocks the binding of U2 auxiliary factor (U2AF) to the polypyrimidine (Py)-tract associated with the 3' splice site of the regulated intron [11].
• U2 auxiliary factor (U2AF) is a non-snRNP protein required for the binding of U2 snRNP to the pre-mRNA branch site [12].

References