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Originally published in Science Express on 8 November 2001
Science 21 December 2001:
Vol. 294. no. 5551, pp. 2507 - 2511
DOI: 10.1126/science.1065961
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Research Articles

A Transcriptional Switch Mediated by Cofactor Methylation

Wei Xu,1 Hongwu Chen,2 Keyong Du,3 Hiroshi Asahara,3 Marc Tini,1 Beverly M. Emerson,4 Marc Montminy,3 Ronald M. Evans15*

We describe a molecular switch based on the controlled methylation of nucleosome and the transcriptional cofactors, the CREB-binding proteins (CBP)/p300. The CBP/p300 methylation site is localized to an arginine residue that is essential for stabilizing the structure of the KIX domain, which mediates CREB recruitment. Methylation of KIX by coactivator-associated arginine methyltransferase 1 (CARM1) blocks CREB activation by disabling the interaction between KIX and the kinase inducible domain (KID) of CREB. Thus, CARM1 functions as a corepressor in cyclic adenosine monophosphate signaling pathway via its methyltransferase activity while acting as a coactivator for nuclear hormones. These results provide strong in vivo and in vitro evidence that histone methylation plays a key role in hormone-induced gene activation and define cofactor methylation as a new regulatory mechanism in hormone signaling.

1 Gene Expression Laboratory,
2 Department of Biological Chemistry, University of California Davis Cancer Center/Basic Science, Sacramento, CA 95817, USA.
3 Peptide Biology Laboratory,
4 Regulatory Biology Laboratory, The Salk Institute for Biological Studies, La Jolla, CA 92037, USA.
5 Howard Hughes Medical Institute, La Jolla, CA 92037, USA.
*   To whom correspondence should be addressed. E-mail: evans{at}salk.edu

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