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Structure, Dynamics, and Function of Staphylococcal Nuclease

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Molecular Science of Fluctuations Toward Biological Functions

Abstract

Protein design principles have been intensively studied using staphylococcal nuclease (SNase) as a model protein. We developed several mutants that take nonnative structures under physiological conditions but still possess enzymatic activity and other mutants that assume stable native structure but are functionally inactive. Using these mutants, we succeeded in decoding the information in the primary sequence. We also describe the nonlocal interactions required for proper folding. Our findings also elucidate the mechanism of ligand-induced folding, which is a good model for coupled folding and binding of intrinsically unfolded proteins.

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Acknowledgment

The author wishes to sincerely thank Prof. H. Kamikubo, Dr. S. Hirano, Dr. H. Nakagawa, Dr. M. Onitsuka, Dr. S. Kato, and Dr. R. Shiba for their help and discussions during this study and Ms. S. Kayamura, Mr. S. Tadokoro, and Mr. R. Nakagaki for their help in making the measurements. This work was supported by a Grant-in-Aid for Scientific Research to MK (15076208, 20370062). The author is especially grateful for the support from a Grant-in-aid for Scientific Research in Innovative Areas (20107006).

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Authors and Affiliations

  1. Graduate School of Materials Science, Nara Institute of Science and Technology, Ikoma, Japan

    Mikio Kataoka

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  1. Mikio Kataoka
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Correspondence to Mikio Kataoka .

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Editors and Affiliations

  1. Kyoto University, Kyoto, Japan

    Masahide Terazima

  2. Nara Institute of Science and Tech, Ikoma, Japan

    Mikio Kataoka

  3. Sojo University, Kumamoto, Japan

    Ryuichi Ueoka

  4. Nagoya University, Nagoya, Japan

    Yuko Okamoto

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Kataoka, M. (2016). Structure, Dynamics, and Function of Staphylococcal Nuclease. In: Terazima, M., Kataoka, M., Ueoka, R., Okamoto, Y. (eds) Molecular Science of Fluctuations Toward Biological Functions . Springer, Tokyo. https://doi.org/10.1007/978-4-431-55840-8_7

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