Solution structure of the DNA-binding domain of MafG

The Maf family proteins, which constitute a subgroup of basic region-leucine zipper (bZIP) proteins, function as transcriptional regulators of cellular differentiation. Together with the

basic region, the Maf extended homology region (EHR), conserved only within the Maf family, defines the DNA binding specific to Mafs. Here we present the first NMR-derived structure of the

DNA-binding domain (residues 1–76) of MafG, which contains the EHR and the basic region. The structure consists of three α-helices and resembles the fold of the DNA-binding domain of Skn-1,

a developmental transcription factor of Caenorhabditis elegans. The structural similarity between MafG and Skn-1 enables us to propose a possible mechanism by which Maf family proteins

recognize their consensus DNA sequences.

We thank E. Arai and F. Arisaka for ultracentrifuge analysis, T. Maeda for useful discussion, K. Yap for providing a program to calculate interhelical angles and T. O'Connor for critical

reading of the manuscript. This work was supported by grants from JSPS and TARA (T.T.); the Ministry of Education, Science, Sports and Culture of Japan (H.M. and M.Y.); JSPS and CREST

(M.Y.); and PROBRAIN (H.M.).

Institute of Basic Medical Science, University of Tsukuba, Tsukuba, 305-8575, Ibaraki, Japan

Hideki Kusunoki, Hozumi Motohashi, Fumiki Katsuoka & Masayuki Yamamoto

Center for Tsukuba Advanced Research Alliance, University of Tsukuba, Tsukuba, 305-8577, Ibaraki, Japan

Hideki Kusunoki, Hozumi Motohashi, Masayuki Yamamoto & Toshiyuki Tanaka

Institute of Applied Biochemistry, University of Tsukuba, Tsukuba, 305-8572, Ibaraki, Japan

Banyu Tsukuba Research Institute, Tsukuba, 300-2611, Ibaraki, Japan

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