SR proteins escort the U4/U6·U5 tri-snRNP to the spliceosome

Robert F. Roscigno, Mariano A. Garcia-Blanco

Research output: Contribution to journalArticlepeer-review

139 Scopus citations


Pre-spliceosomes, formed in HeLa nuclear extracts and isolated by sedimentation on glycerol gradients, were chased into spliceosomes, the macromolecular enzyme that catalyzes intron removal. We demonstrate that the pre-spllceosome to spliceosome transition was dependent on ATP hydrolysis and required both a U-rich small nuclear ribonucleoprotein (U snRNP)-containing fraction and a fraction of non-snRNP factors. The active components in the non-snRNP fraction were identified as SR proteins and were purified to apparent homogeneity. Recombinant SR proteins (ASF, SC35, SRp55), as well as gel-purified SR proteins, with the exception of SRp20, were able to restore efficient spliceosome formation. We also demonstrate that the pre-spliceosome to spliceosome transition requires phosphorylated SR proteins. This is the first evidence that SR proteins are required for the pre-spliceosome to spliceosome transition, the step at which the U4/U6·U5 tri-snRNP assembles on the pre-mRNA. The results shown here, together with previous data, suggest U snRNPs require SR proteins as escorts to enter the assembling spliceosome.

Original languageEnglish (US)
Pages (from-to)692-706
Number of pages15
Issue number7
StatePublished - Dec 1 1995
Externally publishedYes


  • Commitment complex
  • Pre-spliceosome
  • pre-mRNA splicing

ASJC Scopus subject areas

  • Molecular Biology


Dive into the research topics of 'SR proteins escort the U4/U6·U5 tri-snRNP to the spliceosome'. Together they form a unique fingerprint.

Cite this