Role of the Actin Ala-108 - Pro-112 loop in actin polymerization and ATpase activities

Journal of Biological Chemistry

Volumn 287, Issue 52, 2012, Pages 43270-43276

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

^a RIKEN SPring 8 Center   (Japan)

^b NAGOYA UNIVERSITY   (Japan)

^c JAPAN SCIENCE AND TECHNOLOGY AGENCY   (Japan)

^d Aizawa Hospital   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ACCELERATION AND DECELERATION; ACTIN POLYMERIZATION; ARRHENIUS EQUATION; ATOMIC MODELS; ATP-ASE ACTIVITY; CELL FUNCTIONS; CELL PROCESS; ELEMENTARY PROCESS; EUKARYOTIC CELLS; F-ACTIN; FREQUENCY FACTORS; MULTIPLE CONFORMATIONS; POLYMERIZATION PROCESS; SUB-DOMAINS; WEAK INTERACTIONS; WILD TYPES;

ACTIVATION ENERGY; AMINO ACIDS; FLUORINE; NUCLEATION; POLYMERIZATION;

PROTEINS;

ACTIN; ADENOSINE TRIPHOSPHATASE; ALANINE; F ACTIN; G ACTIN; PROLINE;

ACTIN POLYMERIZATION; AMINO ACID SUBSTITUTION; ARTICLE; CONCENTRATION (PARAMETERS); CONFORMATIONAL TRANSITION; ENZYME ACTIVITY; MELTING POINT; MOLECULAR INTERACTION; MUTATION RATE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN STABILITY; STRUCTURE ANALYSIS;

ACTINS; ADENOSINE TRIPHOSPHATASES; AMINO ACID SUBSTITUTION; ANIMALS; AVIAN PROTEINS; CHICKENS; HUMANS; MULTIENZYME COMPLEXES; MUTATION, MISSENSE; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY;

EUKARYOTA;

EID: 84871568349     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.392019     Document Type: Article

References (29)

1. Pollard, T. D. (2007) Regulation of actin filament assembly by Arp2/3 complex and formins. Annu. Rev. Biophys. Biomol. Struct. 36, 451-477
2. Bugyi, B., and Carlier, M. F. (2010) Control of actin filament treadmilling in cell motility. Annu. Rev. Biophys. 39, 449-470
3. Kabsch, W., Mannherz, H. G., Suck, D., Pai, E. F., and Holmes, K. C. (1990) Atomic structure of the actin:DNase I complex. Nature 347, 37-44
4. Holmes, K. C., Popp, D., Gebhard, W., and Kabsch, W. (1990) Atomic model of the actin filament. Nature 347, 44-49
5. Oda, T., Iwasa, M., Aihara, T., Maéda, Y., and Narita, A. (2009) The nature of the globular- to fibrous-actin transition. Nature 457, 441-445
6. Fujii, T., Iwane, A. H., Yanagida, T., and Namba, K. (2010) Direct visualization of secondary structures of F-actin by electron cryomicroscopy. Nature 467, 724-728
7. Otterbein, L. R., Graceffa, P., and Dominguez, R. (2001) The crystal structure of uncomplexed actin in the ADP state. Science 293, 708-711 (Pubitemid 32728675)
8. 137 of actin revealed by recombinant human cardiac muscle α-actinmutants. J. Biol. Chem. 283, 21045-21053
9. Vorobiev, S., Strokopytov, B., Drubin, D. G., Frieden, C., Ono, S., Condeelis, J., Rubenstein, P. A., and Almo, S. C. (2003) The structure of nonvertebrate actin: implications for the ATP hydrolytic mechanism. Proc. Natl. Acad. Sci. U.S.A. 100, 5760-5765 (Pubitemid 36576881)
10. Spudich, J. A., and Watt, S. (1971) The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosintroponin complex with actin and the proteolytic fragments of myosin. J. Biol. Chem. 246, 4866-4871
11. Sano, K., Maeda, K., Oki, M., and Maéda, Y. (2002) Enhancement of protein expression in insect cells by a lobster tropomyosin cDNA leader sequence. FEBS Lett. 532, 143-146 (Pubitemid 35375879)
12. Houk, T. W., Jr., and Ue, K. (1974) The measurement of actin concentration in solution: a comparison of methods. Anal. Biochem. 62, 66-74
13. Nishida, E., and Sakai, H. (1983) Kinetic analysis of actin polymerization. J. Biochem. 93, 1011-1020 (Pubitemid 13042874)
14. Kasai, M. (1969) Thermodynamical aspect of G-F transformations of actin. Biochim. Biophys. Acta 180, 399-409
15. Pollard, T. D. (1983) Measurement of rate constants for actin filament elongation in solution. Anal. Biochem. 134, 406-412
16. Kouyama, T., and Mihashi, K. (1981) Fluorimetry study of N-(1-pyrenyl)-iodoacetamide-labelled F-actin. Local structural change of actin protomer both on polymerization and on binding of heavy meromyosin. Eur. J. Biochem. 114, 33-38 (Pubitemid 11101489)
17. Oosawa, F., Asakura, S., and Ooi, T. (1961) Physical chemistry of muscle protein "actin." Prog. Theor. Phys., Suppl. 17, 14-34
18. Oosawa, F., and Kasai, M. (1962) A theory of linear and helical aggregations of macromolecules. J. Mol. Biol. 4, 10-21
19. irelease following nucleotide hydrolysis in actin or tubulin assembly using 2-amino-6-mercapto-7-methylpurine ribonucleoside and purine-nucleoside phosphorylase as an enzyme-linked assay. Biochemistry 35, 12038 -12045
20. Davis, I. W., Leaver-Fay, A., Chen, V. B., Block, J. N., Kapral, G. J., Wang, X., Murray, L. W., Arendall, W. B., 3rd, Snoeyink, J., Richardson, J. S., and Richardson, D. C. (2007) MolProbity: all-atom contacts and structure validation for proteins and nucleic acids. Nucleic Acids Res. 35, W375-W383
21. Murakami, K., Yasunaga, T., Noguchi, T. Q., Gomibuchi, Y., Ngo, K. X., Uyeda, T. Q., and Wakabayashi, T. (2010) Structural basis for actin assembly, activation of ATP hydrolysis, and delayed phosphate release. Cell 143, 275-287
22. 2+-activation of the regulated actin-activated myosin ATPase observedwith Dictyostelium / Tetrahymena actin chimeras. J. Mol. Biol. 296, 579-595
23. Drenckhahn, D., and Pollard, T. D. (1986) Elongation of actin filaments is a diffusion-limited reaction at the barbed end and is accelerated by inert macromolecules. J. Biol. Chem. 261, 12754-12758 (Pubitemid 17204237)
24. Truhlar, D., and Kohen, A. (2001) Convex Arrhenius plots and their interpretation. Proc. Natl. Acad. Sci. U.S.A. 98, 848-851 (Pubitemid 32121150)
25. Sept, D., and McCammon, J. A. (2001) Thermodynamics and kinetics of actin filament nucleation. Biophys. J. 81, 667-674 (Pubitemid 32721442)
26. Schreiber, G., Haran, G., and Zhou, H. X. (2009) Fundamental aspects of protein-protein association kinetics. Chem. Rev. 109, 839-860
27. Pavlicek, J., Coon, S. L., Ganguly, S., Weller, J. L., Hassan, S. A., Sackett, D. L., and Klein, D. C. (2008) Evidence that proline focuses movement of the floppy loop of arylalkylamine N-acetyltransferase (EC 2.3.1.87). J. Biol. Chem. 283, 14552-14558
28. DeLano, W. L. (2006) The PyMOL Molecular Graphics System, version 0.99, Schrödinger, LLC, New York
29. Caspar, D. L. (1991) Self-control of self-assembly. Curr. Biol. 1, 30-32