The nature of the globular- to fibrous-actin transition

Nature

Volumn 457, Issue 7228, 2009, Pages 441-445

  Oda, Toshiro ^a,b   Iwasa, Mitsusada ^b   Aihara, Tomoki ^a   Maéda, Yuichiro ^b,c   Narita, Akihiro ^c  

^a RIKEN Harima Institute ^*  (Japan)

^b JAPAN SCIENCE AND TECHNOLOGY AGENCY   (Japan)

^c NAGOYA UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ACTIN BINDING PROTEIN; F ACTIN; GLOBULAR PROTEIN; PROTEIN SUBUNIT;

LAGOMORPH; MUSCLE; POLYMERIZATION; PROTEIN; X-RAY DIFFRACTION;

ACTIN POLYMERIZATION; ANIMAL EXPERIMENT; ANIMAL TISSUE; ARTICLE; CELL FUNCTION; CELL MOTILITY; CONFORMATIONAL TRANSITION; DEPOLYMERIZATION; MOLECULAR INTERACTION; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN STRUCTURE; RABBIT; SKELETAL MUSCLE; X RAY DIFFRACTION;

ACTINS; ANIMALS; BIOPOLYMERS; CELL MOVEMENT; GLUTAMINE; HYDROLYSIS; MAGNETICS; MODELS, MOLECULAR; MUSCLE CONTRACTION; MUSCLE, SKELETAL; PROTEIN STRUCTURE, QUATERNARY; PROTEIN SUBUNITS; RABBITS; X-RAY DIFFRACTION;

ORYCTOLAGUS CUNICULUS;

EID: 58749091822     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature07685     Document Type: Article

References (50)

1. Straub, F. B. in Studies Int med Chem Univ Szeged (ed Szent-Györgi), 2, 3-15 (Karger, 1942).
2. Pollard, T. D. & Borisy, G. G. Cellular motility driven by assembly and disassembly of actin filaments. Cell 112, 453-465 (2003).
3. Carlier, M. F. & Pantaloni, D. Control of actin assembly dynamics in cell motility. J. Biol. Chem. 282, 23005-23009 (2007).
4. Oosawa, F. & Asakura, S. Thernodynamics of the Polymerization of Protein (Academic, 1975).
5. Wegner, A. Head to tail polymerization of actin. J. Mol. Biol. 108, 139-150 (1976).
6. Kabsch, W. et al. Atomic structure of the actin:DNase I complex. Nature 347, 37-44 (1990).
7. Holmes, K. C., Popp, D., Gebhard, W. & Kabsch, W. Atomic model of the actin filament. Nature 347, 44-49 (1990).
8. Lorenz, M., Popp, D. & Holmes, K. C. Refinement of the F-actin model against X-ray fiber diffraction data by the use of a directed mutation algorithm. J. Mol. Biol. 234, 826-836 (1993).
9. Tirion, M. M., ben-Avraham, D., Lorenz, M. & Holmes, K. C. Normal modes as refinement parameters for the F-actin model. Biophys. J. 68, 5-12 (1995).
10. Holmes, K. C. et al. Electron cryo-microscopy shows how strong binding of myosin to actin releases nucleotide. Nature 425, 423-427 (2003).
11. Wu, Y. & Ma, J. Refinement of F-actin model against fiber diffraction data by long-range normal modes. Biophys. J. 86, 116-124 (2004).
12. Oda, T. et al. Modeling of the F-actin structure. Adv. Exp. Med. Biol. 592, 385-401 (2007).
13. van den Ent, F., Amos, L. A. & Löwe, J. Prokaryotic origin of the actin cytoskeleton. Nature 413, 39-44 (2001).
14. Joel, P. B., Fagnant, P. M. & Trybus, K. M. Expression of a nonpolymerizable actin mutant in Sf9 cells. Biochemistry 43, 11554-11559 (2004).
15. Wertman, K. F., Drubin, D. G. & Botstein, D. Systematic mutational analysis of the yeast ACT1 gene. Genetics 132, 337-350 (1992).
16. Allingham, J. S., Klenchin, V. A. & Rayment, I. Actin-targeting natural products: structures, properties and mechanisms of action. Cell. Mol. Life Sci. 63, 2119-2134 (2006).
17. Morton, W. M., Ayscough, K. R. & McLaughlin, P. J. Latrunculin alters the actin-monomer subunit interface to prevent polymerization. Nature Cell Biol. 2, 376-378 (2000).
18. Oda, T. et al. Effect of the length and effective diameter of F-actin on the filament orientation in liquid crystalline sols measured by x-ray fiber diffraction. Biophys. J. 75, 2672-2681 (1998).
19. Hayward, S. & Berendsen, H. J. Systematic analysis of domain motions in proteins from conformational change: new results on citrate synthase and T4 lysozyme. Proteins 30, 144-154 (1998).
20. Otterbein, L. R., Graceffa, P. & Dominguez, R. The crystal structure of uncomplexed actin in the ADP state. Science 293, 708-711 (2001).
21. Michie, K. A. & Löwe, J. Dynamic filaments of the bacterial cytoskeleton. Annu. Rev. Biochem. 75, 467-492 (2006).
22. Carballido-Lopez, R. The bacterial actin-like cytoskeleton. Microbiol. Mol. Biol. Rev. 70, 888-909 (2006).
23. Chen, X., Cook, R. K. & Rubenstein, P. A. Yeast actin with a mutation in the "hydrophobic plug" between subdomains 3 and 4 (L266D) displays a cold-sensitive polymerization defect. J. Cell Biol. 123, 1185-1195 (1993).
24. Volkmann, N. et al. The structural basis of myosin V processive movement as revealed by electron cryomicroscopy. Mol. Cell 19, 595-605 (2005).
25. Rould, M. A. et al. Crystal structures of expressed non-polymerizable monomeric actin in the ADP and ATP states. J. Biol. Chem. 281, 31909-31919 (2006).
26. Nolen, B. J. & Pollard, T. D. Insights into the influence of nucleotides on actin family proteins from seven structures of Arp2/3 complex. Mol. Cell 26, 449-457 (2007).
27. Graceffa, P. & Dominguez, R. Crystal structure of monomeric actin in the ATP state. Structural basis of nucleotide-dependent actin dynamics. J. Biol. Chem. 278, 34172-34180 (2003).
28. Robinson, R. C. et al. Crystal structure of Arp2/3 complex. Science 294, 1679-1684 (2001).
29. De La Cruz, E. M. et al. Polymerization and structure of nucleotide-free actin filaments. J. Mol. Biol. 295, 517-526 (2000).
30. Pollard, T. D. Regulation of actin filament assembly by Arp2/3 complex and formins. Annu. Rev. Biophys. Biomol. Struct. 36, 451-477 (2007).
31. Iwasa, M. et al. Dual roles of Q137 of actin revealed by recombinant human cardiac muscle alpha -actin mutants. J. Biol. Chem. 283, 21045-21053 (2008).
32. Vorobiev, S. et al. The structure of nonvertebrate actin: implications for the ATP hydrolytic mechanism. Proc. Natl Acad. Sci. USA 100, 5760-5765 (2003).
33. Vogel, M., Bukau, B. & Mayer, M. P. Allosteric regulation of Hsp70 chaperones by a proline switch. Mol. Cell 21, 359-367 (2006).
34. Yao, X., Nguyen, V., Wriggers, W. & Rubenstein, P. A. Regulation of yeast actin behavior by interaction of charged residues across the interdomain cleft. J. Biol. Chem. 277, 22875-22882 (2002).
35. Nyman, T. et al. The role of MeH73 in actin polymerization and ATP hydrolysis. J. Mol. Biol. 317, 577-589 (2002).
36. Otomo, T. et al. Structural basis of actin filament nucleation and processive capping by a formin homology 2 domain. Nature 433, 488-494 (2005).
37. Furuhashi, K. et al. Phosphorylation by actin kinase of the pointed end domain on the actin molecule. J. Biol. Chem. 267, 9326-9330 (1992).
38. Klenchin, V. A., Khaitlina, S. Y. & Rayment, I. Crystal structure of polymerization-competent actin. J. Mol. Biol. 362, 140-150 (2006).
39. Dalhaimer, P., Pollard, T. D. & Nolen, B. J. Nucleotide-mediated conformational changes of monomeric actin and Arp3 studied by molecular dynamics simulations. J. Mol. Biol. 376, 166-183 (2008).
40. Ravelli, R. B. et al. Insight into tubulin regulation from a complex with colchicine and a stathmin-like domain. Nature 428, 198-202 (2004).
41. Wang, H. W. & Nogales, E. Nucleotide-dependent bending flexibility of tubulin regulates microtubule assembly. Nature 435, 911-915 (2005).
42. Wang, H. & Stubbs, G. Molecular dynamics in refinement against fiber diffraction data. Acta Crystallogr. A 49, 504-513 (1993).
43. Narita, A. & Maeda, Y. Molecular determination by electron microscopy of the actin filament end structure. J. Mol. Biol. 365, 480-501 (2007).
44. Narita, A., Takeda, S., Yamashita, A. & Maeda, Y. Structural basis of actin filament capping at the barbed-end: a cryo-electron microscopy study. EMBO J. 25, 5626-5633 (2006).
45. Kraulis, J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Cryst. 24, 946-950 (1991).
46. Esnouf, R. M. An extensively modified version of MolScript that includes greatly enhanced coloring capabilities. J. Mol. Graph. Model. 15, 132-134 (1997).
47. Merritt, E. A. & Bacon, D. J. Raster3D: photorealistic molecular graphics. Methods Enzymol. 277, 505-524 (1997).
48. Kudryashov, D. S. et al. The crystal structure of a cross-linked actin dimer suggests a detailed molecular interface in F-actin. Proc. Natl Acad. Sci. USA 102, 13105-13110 (2005).
49. Allingham, J. S., Zampella, A., D'Auria, M. V. & Rayment, I. Structures of microfilament destabilizing toxins bound to actin provide insight into toxin design and activity. Proc. Natl Acad. Sci. USA 102, 14527-14532 (2005).
50. Rizvi, S. A., Tereshko, V., Kossiakoff, A. A. & Kozmin, S. A. Structure of bistramide A-actin complex at a 1.35 angstroms resolution. J. Am. Chem. Soc. 128, 3882-3883 (2006).