The spliceosome assembly pathway in mammalian extracts.

Journal Article

A mammalian splicing commitment complex was functionally defined by using a template commitment assay. This complex was partially purified and shown to be a required intermediate for complex A formation. The productive formation of this commitment complex required both splice sites and the polypyrimidine tract. U1 small nuclear ribonucleoprotein (snRNP) was the only spliceosomal U snRNP required for this formation. A protein factor, very likely U2AF, is probably involved in the formation of the splicing commitment complex. From the kinetics of appearance of complex A and complex B, it was previously postulated that complex A represents a functional intermediate in spliceosome assembly. Complex A was partially purified and shown to be a required intermediate for complex B (spliceosome) formation. Thus, a spliceosome pathway is for the first time supported by direct biochemical evidence: RNA+U1 snRNP+?U2 auxiliary factor+?Y----CC+U2 snRNP+Z----A+U4/6,5 snRNPs+ beta----B.

Full Text

Duke Authors

Cited Authors

  • Jamison, SF; Crow, A; Garcia-Blanco, MA

Published Date

  • October 1992

Published In

Volume / Issue

  • 12 / 10

Start / End Page

  • 4279 - 4287

PubMed ID

  • 1383687

International Standard Serial Number (ISSN)

  • 0270-7306

Language

  • eng

Conference Location

  • United States