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The cavity in the hydrophobic core of Myb DNA-binding domain is reserved for DNA recognition and trans-activation

Nature Structural Biology volume 3, pages 178–187 (1996)Cite this article

Abstract

The DNA-binding domain of Myb consists of three imperfect repeats, R1, R2 and R3, each containing a helix-turn-helix motif variation. Among these repeats, R2 has distinct characteristics with high thermal instability. The NMR structure analysis found a cavity inside the hydrophobic core of R2 but not in R1 or R3. Here, we show that R2 has slow conformational fluctuations, and that a cavity-filling mutation which stabilizes the R2 structure significantly reduces specific Myb DNA-binding activity and trans-activation. Structural observations of the free and DNA-complexed states suggest that the implied inherent conformational flexibility of R2, associated with the presence of the cavity, could be important for DNA recognition by Myb.

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Authors and Affiliations

  1. Tsukuba Life Science Center, The Institute of Physical and Chemical Research (RIKEN), 3-1-1 Koyadai, Tsukuba, Ibaraki, 305, Japan

    Kazuhiro Ogata, Chie Kanei-Ishii, Shunsuke Ishii & Akinori Sarai

  2. Graduate School of Integrated Science, Yokohama City University, 22-2 Seto, Kanazawa-ku, Yokohama, 236, Japan

    Kazuhiro Ogata, Motoko Sasaki, Aritaka Nagadoi, Masato Enari & Yoshifumi Nishimura

  3. Department of Molecular Physiology, The Tokyo Metropolitan Institute of Medical Science, 3-18-22 Honkomagome, Bunkyo-ku, Tokyo, 113, Japan

    Hideki Hatanaka

  4. Protein Engineering Research Institute, 6-2-3 Furuedai, Suita, Osaka, 565, Japan

    Haruki Nakamura

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Ogata, K., Kanei-Ishii, C., Sasaki, M. et al. The cavity in the hydrophobic core of Myb DNA-binding domain is reserved for DNA recognition and trans-activation. Nat Struct Mol Biol 3, 178–187 (1996). https://doi.org/10.1038/nsb0296-178

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