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Enhanced phosphorylation of the C-terminal domain of RNA polymerase II upon serum stimulation of quiescent cells: possible involvement of MAP kinases.

1994; Springer Nature; Volume: 13; Issue: 20 Linguagem: Inglês

10.1002/j.1460-2075.1994.tb06804.x

1460-2075

M.-F. Dubois, Văn Thành Nguyễn, Michael Dahmus, Gilles Pagès, Jacques Pouysségur, Olivier Bensaude,

Protein Kinase Regulation and GTPase Signaling

Research Article17 October 1994free access Enhanced phosphorylation of the C-terminal domain of RNA polymerase II upon serum stimulation of quiescent cells: possible involvement of MAP kinases. M.F. Dubois M.F. Dubois Laboratoire de Génétique Moléculaire, URA CNRS no. 1302, Paris, France. Search for more papers by this author V.T. Nguyen V.T. Nguyen Laboratoire de Génétique Moléculaire, URA CNRS no. 1302, Paris, France. Search for more papers by this author M.E. Dahmus M.E. Dahmus Laboratoire de Génétique Moléculaire, URA CNRS no. 1302, Paris, France. Search for more papers by this author G. Pagès G. Pagès Laboratoire de Génétique Moléculaire, URA CNRS no. 1302, Paris, France. Search for more papers by this author J. Pouysségur J. Pouysségur Laboratoire de Génétique Moléculaire, URA CNRS no. 1302, Paris, France. Search for more papers by this author O. Bensaude O. Bensaude Laboratoire de Génétique Moléculaire, URA CNRS no. 1302, Paris, France. Search for more papers by this author M.F. Dubois M.F. Dubois Laboratoire de Génétique Moléculaire, URA CNRS no. 1302, Paris, France. Search for more papers by this author V.T. Nguyen V.T. Nguyen Laboratoire de Génétique Moléculaire, URA CNRS no. 1302, Paris, France. Search for more papers by this author M.E. Dahmus M.E. Dahmus Laboratoire de Génétique Moléculaire, URA CNRS no. 1302, Paris, France. Search for more papers by this author G. Pagès G. Pagès Laboratoire de Génétique Moléculaire, URA CNRS no. 1302, Paris, France. Search for more papers by this author J. Pouysségur J. Pouysségur Laboratoire de Génétique Moléculaire, URA CNRS no. 1302, Paris, France. Search for more papers by this author O. Bensaude O. Bensaude Laboratoire de Génétique Moléculaire, URA CNRS no. 1302, Paris, France. Search for more papers by this author Author Information M.F. Dubois1, V.T. Nguyen1, M.E. Dahmus1, G. Pagès1, J. Pouysségur1 and O. Bensaude1 1Laboratoire de Génétique Moléculaire, URA CNRS no. 1302, Paris, France. The EMBO Journal (1994)13:4787-4797https://doi.org/10.1002/j.1460-2075.1994.tb06804.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info The largest subunit of RNA polymerase (RNAP) II contains at it C-terminus an unusual domain comprising tandem repeats of the consensus sequence Tyr-Ser-Pro-Thr-Ser-Pro-Ser. This C-terminal domain (CTD) can undergo phosphorylation at multiple sites giving rise to a form of the enzyme designated RNAP IIO. The unphosphorylated form is designated RNAP IIA. The largest subunits of RNAPs IIO and IIA are designated IIo and IIa, respectively. In quiescent NIH 3T3 fibroblasts, subunits IIo and IIa are present in comparable amounts. Upon serum stimulation, the amount of subunit IIo increases markedly and remains elevated for several hours. The increase of subunit IIo also occurs in transcription-inhibited cells and, therefore, is not a consequence of serum-activated transcription. This observation suggests that serum stimulation activates a CTD kinase and/or inhibits a CTD phosphatase. This hypothesis is supported by the finding that serum stimulates phosphorylation of a beta-galactosidase-CTD fusion protein expressed in these cells. Furthermore, an enhanced CTD kinase activity was discovered in lysates from serum-stimulated fibroblasts and was found to copurify with MAP kinases on a Mono Q column and to bind to anti-MAP kinase antibodies. The idea that MAP kinases phosphorylate the CTD in vivo is supported by the observation that subunit IIa, but not subunit IIb which lacks the CTD, is phosphorylated at multiple sites by purified MAP kinase. Consequently, the MAP kinases are a new class of CTD kinases which appear to be involved in the phosphorylation of RNAP II following serum stimulation. This phosphorylation may contribute to the transcriptional activation of serum-stimulated genes. Previous ArticleNext Article Volume 13Issue 201 October 1994In this issue RelatedDetailsLoading ...