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Solution structure of the DNA-binding domain of MafG

Nature Structural Biology volume 9, pages 252–256 (2002)Cite this article

Abstract

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.

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Figure 1: DNA recognition by MafG(1–76).
Figure 2: 3D structure of MafG(1–76).
Figure 3: Chemical shift changes of amide protons (upper panel) and nitrogens (lower panel) of MafG(1–76) upon binding to the DNA containing the T-MARE-like sequence.
Figure 4: Comparison of MafG(1–76) with the Skn-1 DNA-binding domain.

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Acknowledgements

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.).

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Authors and Affiliations

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

    Hideki Kusunoki, Hozumi Motohashi, Fumiki Katsuoka & Masayuki Yamamoto

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

    Hideki Kusunoki, Hozumi Motohashi, Masayuki Yamamoto & Toshiyuki Tanaka

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

    Akio Morohashi & Toshiyuki Tanaka

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

    Akio Morohashi

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  1. Hideki Kusunoki
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Correspondence to Toshiyuki Tanaka.

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Kusunoki, H., Motohashi, H., Katsuoka, F. et al. Solution structure of the DNA-binding domain of MafG. Nat Struct Mol Biol 9, 252–256 (2002). https://doi.org/10.1038/nsb771

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