Yahli Lorch1, Jenny Beve2,
Claes M. Gustafsson2, Lawrence C. Myers3, and Roger
D. Kornberg1
1 Department
of Structural Biology, Stanford School of Medicine, Stanford, California
94305
2 Department
of Medical Nutrition, Karolinska Institute, NOVUM, S-141 86 Huddinge, Sweden
3 Department
of Biochemistry, Dartmouth Medical School, Hanover, New Hampshire 03755
Corresponding
author: Roger D. Kornberg1, 650 723 6988 (phone), 650 723 8464
(fax),
E-mail: kornberg@stanford.edu
Mediator, a multiprotein complex involved in the regulation of RNA polymerase II transcription, binds to nucleosomes and acetylates histones. Three lines of evidence identify the Nut1 subunit of Mediator as responsible for the histone acetyltransferase (HAT) activity. An ''in-gel'' HAT assay reveals a single band of the appropriate size. Sequence alignment shows significant similarity of Nut1 to the GCN5-related N-acetyltransferase superfamily. Finally, recombinant Nut1 exhibits HAT activity in an in-gel assay.
1. "Mated Models of Gene Regulation in Eukaryotes".
2. "Oncogenes as Molecular Targets within Active Chromatin".