Function
Pre-mRNA-splicing factors (Prp) are the proteins which associate with mRNA at its various splicing sites to produce alternative splicing[1].
- Prp3b is part of the U2 small nuclear ribonucleoproteins complex (U2 snRNP)
- Prp8 functions as a scaffold which mediates the ordered assembly of spliceosomal proteins and snRNAs. For details see Prp8
- Prp18 and Bud31 are essential for the catalytic step in pre-mRNA splicing process.
- snRNA-associated-splicing factor 24 binds preferentially to the U4/U6 hybrid snRNAs. For details see Prp24
- For Prp19 see Prp19
- For Prp20 see Srp20-Human Alternative Splicing Factor
- Prp31 functions in forming the U4/U5-U6 tri-snRNP.
- For Prp40 see Prp40.
- Prpcwc2 is a yeast splicing factor which plays a role in the generation of a functional splicing center Prp RBM22 is the human homolog of Prpcwc2.
- Prpcwc26 or Bud13 belongs to the pre-mRNA retention and splicing complex RES.
Disease
Mutations in Prp8 and Prp31 cause retinitis pigmentosa[2].
Structural highlights
Prp8 is a multi-domain protein containing an RNA-binding domain and a Jab1/MPN domain.
3D Structures of pre-mRNA splicing factors
Pre-mRNA splicing factors 3D structures
- ↑ Misteli T, Spector DL. RNA polymerase II targets pre-mRNA splicing factors to transcription sites in vivo. Mol Cell. 1999 Jun;3(6):697-705. PMID:10394358
- ↑ McKie AB, McHale JC, Keen TJ, Tarttelin EE, Goliath R, van Lith-Verhoeven JJ, Greenberg J, Ramesar RS, Hoyng CB, Cremers FP, Mackey DA, Bhattacharya SS, Bird AC, Markham AF, Inglehearn CF. Mutations in the pre-mRNA splicing factor gene PRPC8 in autosomal dominant retinitis pigmentosa (RP13). Hum Mol Genet. 2001 Jul 15;10(15):1555-62. PMID:11468273
