Nucleic Acids Research, 1992, Vol. 20, No. 19 5197-5204
© 1992
MOLECULAR BIOLOGY |
Differential ASF/SF2 activity in extracts from normal WI38 and transformed WI38VA13 cells
Département de Microbiologie, Faculté de Médecine, Université de Sherbrooke Sherbrooke, Québec J1H 5N4, Canada
Received April 9, 1992. Revised August 29, 1992. Accepted August 29, 1992.
The normal human fibroblast cell line WI38 and a transformed derivative, WI38VA13, differentially splice flbronectin pre-mRNA in vivo. As a first step to understand the molecular basis for this regulation of splicing, we examined the ability of WI38 and WI38VA13 nuclear extracts to splice model adenovirus and globln pre-mRNAs. Adenovirus RNA splicing was detected in WI38VA13 but not in WI38 extracts. Likewise, when supplemented with a HeLa post-nuclear supernatant (S100), human ß-globin RNA splicing was detected in WI38VA13 but not in WI38 extracts. The splicing defect in WI38 extracts was associated with a reduced ability to form splicing complexes and with a corresponding decrease in the interaction of U2 small nuclear ribonucleoprotein (snRNP) with the branchsite. These defects did not correlate with a decrease in 65 kD U2AF binding since equivalent U2AF level and activity were detected in WI38 and WI38VA13 extracts. Rather, WI38 extracts displayed reduced ASF/SF2 activity and contained a low level of 30 and 40 kD SR phosphoprotelns. Moreover, addition of purified ASF/SF2 dramatically increased splicing complex formation in WI38 extracts. These results raise the possibility that variations in the level and activity of ASF/SF2 and other SR proteins play a role in the regulation of flbronectin splicing.
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