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Nucleic Acids Research, 2001, Vol. 29, No. 7 1524-1533
© 2001 Oxford University Press

Transcriptional adaptor and histone acetyltransferase proteins in Arabidopsis and their interactions with CBF1, a transcriptional activator involved in cold-regulated gene expression

Eric J. Stockinger, Yaopan Mao1, Martha K. Regier1, Steven J. Triezenberg1 and Michael F. Thomashow*

Department of Crop and Soil Sciences and 1Department of Biochemistry, Michigan State University, East Lansing, MI 48824, USA

The Arabidopsis CBF transcriptional activators bind to the CRT/DRE regulatory element present in the promoters of many cold-regulated genes and stimulate their transcription. Expression of the CBF1 proteins in yeast activates reporter genes carrying a minimal promoter with the CRT/DRE as an upstream regulatory element. Here we report that this ability of CBF1 is dependent upon the activities of three key components of the yeast Ada and SAGA complexes, namely the histone acetyltransferase (HAT) Gcn5 and the transcriptional adaptor proteins Ada2 and Ada3. This result suggested that CBF1 might function through the action of similar complexes in Arabidopsis. In support of this hypothesis we found that Arabidopsis has a homolog of the GCN5 gene and two homologs of ADA2, the first report of multiple ADA2 genes in an organism. The Arabidopsis GCN5 protein has intrinsic HAT activity and can physically interact in vitro with both the Arabidopsis ADA2a and ADA2b proteins. In addition, the CBF1 transcriptional activator can interact with the Arabidopsis GCN5 and ADA2 proteins. We conclude that Arabidopsis encodes HAT-containing adaptor complexes that are related to the Ada and SAGA complexes of yeast and propose that the CBF1 transcriptional activator functions through the action of one or more of these complexes.

* To whom correspondence should be addressed. Tel: +1 517 355 2299; Fax: +1 517 353 5174; Email: thomash6{at}msu.edu Present address: Eric J. Stockinger, Department of Horticulture and Crop Science, 209 Williams Hall, The Ohio State University/OARDC, Wooster, OH 44691, USA


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