Nucleic Acids Research, 1995, Vol. 23, No. 16 3206-3213
© 1995
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The nuclear matrix phosphoprotein p255 associates with splicing complexes as part of the [U4/Y6.U5]tri-snRNP particle
Dèpartment de Microbiologie, Facultè de Mèdecine, Universitè de Sherbrooks Sherbrooke, Quèbec J1H 5n4, Canada 1Centre de Recherche du CHUL Canada 2Dèpartment de Mèdecine, Universitè Laval Sainte-Foy, Quèbec G1V 4G2, Canada
*To whom correspondence should be addressed
Received May 10, 1995. Accepted July 12, 1995.
The monoclonal antibody CC3 recognizes a phosphorylated epttope present on an Interphase protein of 255 kDa. Previous work has shown that p255 is localized mainly to nuclear speckles and remains associated with the nuclear matrix scaffold following extraction with non-Ionic detergents, nucleases and high salt. The association of p255 with splicing complexes is suggested by the finding that mAb CC3 can inhibit in vitro splicing and immunoprecipitate pre-messenger RNA and splicing products. Small nuclear RNA immunopreclpttation assays show that p255 is a component of the U5 small nuclear ribonucleoprotein (snRNP) and the [U4/U6.U5] trl-snRNP complex. In RNase protection assays, mAb CC3 immunoprecipttates fragments containing branch site and 3' splice site sequences. As predicted for a [U4/U6.U5]associated component, the recovery of the branch site-protected fragment requires binding of U2 snRNP and is inhibited by EDTA. p255 may correspond to the previously identified p220 protein, the mammalian analogue of the yeast PRP8 protein. Our results suggest that changes in the phosphorylation of p255 may be part of control mechanisms that interface splicing activity with nuclear organization.
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