Discovery of ultrafast myosin, its amino acid sequence, and structural features

Author:

Haraguchi Takeshi1ORCID,Tamanaha Masanori1,Suzuki Kano2ORCID,Yoshimura Kohei1,Imi Takuma1ORCID,Tominaga Motoki34ORCID,Sakayama Hidetoshi5,Nishiyama Tomoaki6,Murata Takeshi278ORCID,Ito Kohji17ORCID

Affiliation:

1. Department of Biology, Graduate School of Science, Chiba University, Chiba 263-8522, Japan

2. Department of Chemistry, Graduate School of Science, Chiba University, Chiba 263-8522, Japan

3. Faculty of Education and Integrated Arts and Sciences, Waseda University, Shinjuku-ku, Tokyo 162-8480, Japan

4. Department of Integrative Bioscience and Biomedical Engineering, Graduate School of Science and Engineering, Waseda University, Shinjuku-ku, Tokyo 162-8480, Japan

5. Department of Biology, Graduate School of Science, Kobe University, Nada-ku, Kobe 657-8501, Japan

6. Research Center for Experimental Modeling of Human Disease, Kanazawa University, Kanazawa 920-0934, Japan

7. Membrane Protein Research and Molecular Chirality Research Center, Chiba University, Chiba 263-8522, Japan

8. Structure Biology Research Center, Institute of Materials Structure Science, High Energy Accelerator Research Organization (KEK), Tsukuba 305-0801, Japan

Abstract

Significance It has been suggested for more than 50 y that the fastest myosin in the biological world with a velocity of 70 μm s −1 exists in the alga Chara , because cytoplasmic streaming with a velocity of 70 μm s −1 occurs in Chara cells. However, a myosin with that velocity has not yet been identified. In this work, we succeeded in cloning a myosin XI with a velocity of 60 μm s −1 , which was measured using a chimeric myosin. We also successfully crystallized myosin XI. Structural comparison of various myosins and mutation experiments of actin-binding regions suggests that the central regions that define the fast movement of Chara myosin XI are the actin-binding sites.

Publisher

Proceedings of the National Academy of Sciences

Subject

Multidisciplinary

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