Article | Published:

The nature of the globular- to fibrous-actin transition

Nature volume 457, pages 441445 (22 January 2009) | Download Citation

  • A Corrigendum to this article was published on 24 September 2009

Abstract

Actin plays crucial parts in cell motility through a dynamic process driven by polymerization and depolymerization, that is, the globular (G) to fibrous (F) actin transition. Although our knowledge about the actin-based cellular functions and the molecules that regulate the G- to F-actin transition is growing, the structural aspects of the transition remain enigmatic. We created a model of F-actin using X-ray fibre diffraction intensities obtained from well oriented sols of rabbit skeletal muscle F-actin to 3.3 Å in the radial direction and 5.6 Å along the equator. Here we show that the G- to F-actin conformational transition is a simple relative rotation of the two major domains by about 20 degrees. As a result of the domain rotation, the actin molecule in the filament is flat. The flat form is essential for the formation of stable, helical F-actin. Our F-actin structure model provides the basis for understanding actin polymerization as well as its molecular interactions with actin-binding proteins.

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Accessions

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Protein Data Bank

Data deposits

The coordinates for F-actin model have been submitted to PDB under accession number 2ZWH.

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Acknowledgements

We thank K. C. Holmes for continuous encouragement and D. Hanein for the gift of the atomic coordinates of the Volkmann et al. model (ref. 24). We thank K. Namba, K. Makino and K. Hasegwa for comments on the manuscript, the gift of software package for the fibre analysis and help with recording the diffraction patterns. We also thank S. Fujiwara and K. Mihashi for comments on the manuscript. We finally thank beam-line staffs at SPring-8 BL40B2, BL41XU and BL45XU-SAX, especially M. Kawamoto and K. Ito. The electron microscopy section of this study is partially supported by the Kazato Research Foundation (A.N.).

Author Contributions The X-ray fibre diffraction analysis for F-actin structure was performed by T.O. The mutant analysis of actin was conducted by M.I. and T.A. The structural analysis for the F-actin structure by the use of the electron cryomicroscopy analysis was conducted by A.N. Manuscript preparation was done by T.O. together with Y.M.

Author information

Affiliations

  1. X-ray Structural Analysis Research Team, RIKEN SPring-8 Center, RIKEN Harima Institute, 1-1-1, Kouto, Sayo, Hyogo 679-5148, Japan

    • Toshiro Oda
    •  & Tomoki Aihara
  2. ERATO project ‘Actin-filament dynamics’, Japan Science and Technology Agency (JST), 1-1-1, Kouto, Sayo, Hyogo 679-5148, Japan

    • Toshiro Oda
    • , Mitsusada Iwasa
    •  & Yuichiro Maéda
  3. Structural Biology Research Center and Division of Biological Science, Graduate School of Science, Nagoya University, Furo, Nagoya 464-8601, Japan

    • Yuichiro Maéda
    •  & Akihiro Narita

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Corresponding author

Correspondence to Toshiro Oda.

Supplementary information

PDF files

  1. 1.

    Supplementary Information

    This file contains Supplementary Figures 1-9 with Legends, and Supplementary References, Supplementary Methods with Supplementary Methods Figures 1-5 with Legends and Supplementary Methods References.

Text files

  1. 1.

    Atomic coordinates 1

    This file contains the atomic coordinates 1-monomer.pdb

  2. 2.

    Atomic coordinates 2

    This file contains the atomic coordinates 3- monomer.pdb

Videos

  1. 1.

    Supplementary Video 1

    Supplementary Video 1 shows comparison of our F-actin model and the Holmes 2003 model with the EM map. (See nature07685-s1 for full movie legend).

  2. 2.

    Supplementary Video 2

    Supplementary Video 2 shows comparison of our F-actin model and the Volkmann model with the EM map.(See nature07685-s1 for full movie legend).

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DOI

https://doi.org/10.1038/nature07685

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