PRP8, also designated pre-mRNA-processing-splicing factor 8, is a highly conserved nuclear protein and a central component of the catalytic core of the spliceosome, where it may be involved in various molecular rearrangements. PRP8, which is widely expressed, plays a role in transesterification reactions that regulate splicesome-induced pre-mRNA splicing. Specifically, PRP8 interacts with the GU dinucleotide at the 5' splice site (5'SS) and forms a specific UV-inducible cross-link. It also interacts functionally with the 3'SS, affecting the efficiency of the second catalytic step. PRP8 may play a role in the first transesterification step, as PRP8 mutations that prohibit negative regulation of PRP28 or PRP44/Brr2 subsequently block U4 activation. In addition, PRP8 interacts with a conserved region of U6 that is instrumental in the formation of the catalytic core of the spliceosome.
