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PRPF18  -  pre-mRNA processing factor 18

Homo sapiens

Synonyms: HPRP18, PRP18, PRP18 homolog, Pre-mRNA-splicing factor 18, hPRP18, ...
 
 
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High impact information on PRPF18

  • Splicing activity can be restored to hPrp18-depleted HeLa cell extracts by yeast Prp18, showing that important functional regions of the proteins have been conserved [1].
  • The hPrp18 protein is bound tightly to the spliceosome only during the second step of splicing. hPrp18 is required for the splicing of several pre-mRNAs, making it the first general second-step splicing factor found in humans [1].
  • A 55-kD protein that cross-reacts with antibodies against hPrp18 is a constituent of the U4/U6 and U4/U6 x U5 snRNP particles [1].
  • USA-CyP forms separate, stable complexes with hPrp18 and hPrp4 in which the active site of the cyclophilin is exposed [2].
  • The cyclophilin inhibitor cyclosporin A slows pre-mRNA splicing in vitro, and we show that its inhibition of the second step of splicing is caused by blocking the action of USA-CyP within its complex with hPrp18 [2].
 

Biological context of PRPF18

  • The spliceosomal cyclophilin H is a specific component of the human U4/U6 small nuclear ribonucleoprotein particle, interacting with homologous sequences in the proteins U4/U6-60K and hPrp18 during pre-mRNA splicing [3].
 

Anatomical context of PRPF18

  • In HeLa cell extracts immunodepleted of hPrp18, the second step of pre-mRNA splicing is abolished [1].

References

  1. A human protein required for the second step of pre-mRNA splicing is functionally related to a yeast splicing factor. Horowitz, D.S., Krainer, A.R. Genes Dev. (1997) [Pubmed]
  2. A cyclophilin functions in pre-mRNA splicing. Horowitz, D.S., Lee, E.J., Mabon, S.A., Misteli, T. EMBO J. (2002) [Pubmed]
  3. Crystal structure of a complex between human spliceosomal cyclophilin H and a U4/U6 snRNP-60K peptide. Reidt, U., Wahl, M.C., Fasshauer, D., Horowitz, D.S., Lührmann, R., Ficner, R. J. Mol. Biol. (2003) [Pubmed]
 
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