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Mol Cell Biol. 1992 October; 12(10): 4279-4287

The spliceosome assembly pathway in mammalian extracts.

S F Jamison, A Crow and M A Garcia-Blanco

Department of Microbiology and Immunology, Duke University Medical Center, Durham, North Carolina 27710.

ABSTRACT

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.

Mol Cell Biol. 1992 October; 12(10): 4279-4287




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