Nucleic Acids Research, Vol 24, Issue 23 4649-4652, Copyright © 1996 by Oxford University Press
M Vincent, P Lauriault, MF Dubois, S Lavoie, O Bensaude and B Chabot
The monoclonal antibody CC-3 recognizes a phosphodependent epitope on a 255
kDa nuclear matrix protein (p255) recently shown to associate with splicing
complexes as part of the [U4/U6.U5] tri-snRNP particle [Chabot et al.
(1995) Nucleic Acids Res. 23, 3206-3213]. In mouse and Drosophila cultured
cells the electrophoretic mobility of p255, faster in the latter species,
was identical to that of the hyperphosphorylated form of RNA polymerase II
largest subunit (IIo). The CC-3 immunoreactivity of p255 was abolished by
5,6-dichloro-1-beta-D- ribofuranosylbenzimidazole, which is known to cause
the dephosphorylation of the C-terminal domain of subunit IIo by inhibiting
the TFIIH-associated kinase. The identity of p255 was confirmed by showing
that CC-3-immunoprecipitated p255 was recognized by POL3/3 and 8WG16, two
antibodies specific to RNA polymerase II largest subunit. Lastly, the
recovery of RNA polymerase II largest subunit from HeLa splicing mixtures
was compromised by EDTA, which prevents the interaction of p255 with
splicing complexes and inhibits splicing. Our results indicate that p255
represents a highly phosphorylated form of RNA polymerase II largest
subunit physically associated with spliceosomes and possibly involved in
coupling transcription to RNA processing.
ARTICLES
The nuclear matrix protein p255 is a highly phosphorylated form of RNA polymerase II largest subunit which associates with spliceosomes
Departement de Medecine, Recherche en Sciences de la Vie et de la Sante, Universite Laval, Ste-Foy, Quebec, Canada. mvincent@rsvs.ulaval.ca
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