In the assembly of a prespliceosome, U2 small nuclear ribonucleoprotein (snRNP) functions in pre-messenger RNA (mRNA) splicing together with splicing factors (SFs) 3a, SF3b, and several other proteins. The 17S but not the 12S form of U2 snRNP is active in splicing-complex formation. Here it is shown that the SF3a subunits correspond to three of the 17S U2 snRNP-specific polypeptides. SF3a interacts with U2 snRNP in the presence of SF3b to generate a structure similar to 17S U2 snRNP, which suggests a function for SF3a and SF3b in the incorporation of U2 snRNP into the spliceosome. Furthermore, the 60-kilodalton subunit of SF3a is related to the yeast splicing protein PRP9.

A cDNA encoding the 60 kDa subunit of mammalian splicing factor SF3a has been isolated. The deduced protein sequence reveals a 30% identity to the PRP9 splicing protein of the yeast S.cerevisiae. The highest homology is present in a zinc finger-like region in the C-terminal domain of both proteins. The PRP9 zinc finger-like motif has been replaced by the equivalent region of mammalian SF3a60. The chimeric protein rescues the temperature-sensitive phenotype of the prp9-1 mutant strain demonstrating that not only the structure but also the function of this domain has been conserved during evolution.

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