Nucleic Acids Research, Vol 27, Issue 22 4399-4404, Copyright © 1999 by Oxford University Press
F Bonnet, M Vigneron, O Bensaude and MF Dubois
The largest subunit of the mammalian RNA polymerase II possesses a C-
terminal domain (CTD) consisting of 52 repeats of the consensus sequence,
Tyr(1)-Ser(2)-Pro(3)-Thr(4)-Ser(5)-Pro(6)-Ser(7). Phosphorylation of the
CTD is known to play a key role in gene expression. We now show that
treatments such as osmotic and oxidative shocks or serum stimulation
generate a new type of phosphorylated subunit, the IIm form. This IIm form
might be generated in vivo by ERK- type MAP kinase phosphorylation as: (i)
ERK1/2 are major CTD kinases found in cell extracts; (ii) the
immunoreactivity of the IIm form against a panel of monoclonal antibodies
indicates that the CTD is exclusively phosphorylated on Ser-5 in the
repeats, like RNA polymerase II phosphorylated in vitro by an ERK1/2; and
(iii) the IIm form does not appear when ERK activation is prevented by
treating cells with low concentrations of highly specific inhibitors of
MEK1/2. Since the IIm subunit is not affected by inhibition of
transcription and is not bound to chromatin, it does not participate in
transcription.
ARTICLES
Transcription-independent phosphorylation of the RNA polymerase II C- terminal domain (CTD) involves ERK kinases (MEK1/2)
Laboratoire de Regulation de l'Expression Genetique, CNRS UMR 8541, Ecole Normale Superieure, 46 rue d'Ulm, 75230 Paris Cedex 05, France.
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