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J. Biol. Chem., Vol. 281, Issue 39, 28964-28974, September 29, 2006

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An ACT-like Domain Participates in the Dimerization of Several Plant Basic-helix-loop-helix Transcription Factors^*

Antje Feller¹, J. Marcela Hernandez¹, and Erich Grotewold^¶2

From the Molecular, Cellular, and Developmental Biology Program, the Ohio State Biochemistry Program, and ^¶the Department of Plant Cellular and Molecular Biology and Plant Biotechnology Center, Ohio State University, Columbus, Ohio 43210

The maize basic-helix-loop-helix (bHLH) factor R belongs to a group of proteins with important functions in the regulation of metabolism and development through the cooperation with R2R3-MYB transcription factors. Here we show that in addition to the bHLH and the R2R3-MYB-interacting domains, R contains a dimerization region located C-terminal to the bHLH motif. This protein-protein interaction domain is important for the regulation of anthocyanin pigment biosynthesis by contributing to the recruitment of the C1 R2R3-MYB factor to the C1 binding sites present in the promoters of flavonoid biosynthetic genes. The R dimerization region bares structural similarity to the ACT domain present in several metabolic enzymes. Protein fold recognition analyses resulted in the identification of similar ACT-like domains in several other plant bHLH proteins. We show that at least one of these related motifs is capable of mediating homodimer formation. These findings underscore the function of R as a docking site for multiple protein-protein interactions and provide evidence for the presence of a novel dimerization domain in multiple plant bHLH proteins.

Received for publication, April 5, 2006 , and in revised form, July 24, 2006.

^* This work was supported by the National Research Initiative of the United States Department of Agriculture Cooperative State Research, Education, and Extension Service Grant 2003-35318-13689 (to E. G.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ These authors contributed equally to this work and are listed in alphabetical order.

² To whom correspondence should be addressed: Dept. of Plant Cellular and Molecular Biology and Plant Biotechnology Center, The Ohio State University, 206 Rightmire Hall, 1060 Carmack Rd., Columbus, OH 43210. Tel.: 614-292-2483; Fax: 614-292-5379; E-mail: grotewold.1{at}osu.edu.

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