The association of actin and myosin in the presence of γ-amido-ATP proceeds mainly via a complex with myosin in the closed conformation

Biochemistry

Volumn 46, Issue 33, 2007, Pages 9654-9664

  Jahn, Werner ^a  

^a MAX PLANCK INSTITUTE FOR MEDICAL RESEARCH   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

CLEAVAGE; CROSS-BRIDGE CYCLE; INTERMEDIATES; MYOSIN;

ADENOSINETRIPHOSPHATE; AMINO ACIDS; CONFORMATIONS; DISSOCIATION; FLUORESCENCE; HYDROLYSIS; LIGHT SCATTERING; NUCLEOTIDES; QUENCHING;

PROTEINS;

ACTIN; ADENOSINE TRIPHOSPHATE DERIVATIVE; GAMMA AMIDOADENOSINE TRIPHOSPHATE; MYOSIN; UNCLASSIFIED DRUG;

ACTIN MYOSIN INTERACTION; ARTICLE; FLUORESCENCE; LIGHT SCATTERING; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CONFORMATION; STRUCTURE ANALYSIS;

ACTINS; ADENOSINE DIPHOSPHATE; ADENYLYL IMIDODIPHOSPHATE; ANIMALS; ANTHRANILIC ACIDS; DICTYOSTELIUM; FLUORESCENCE; MYOSINS; PROTEIN CONFORMATION; SPECTROMETRY, FLUORESCENCE; TRYPTOPHAN;

EID: 34548061261     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi700318t     Document Type: Article

References (21)

1. Geeves, M. A., and Holmes, K. C. (1999) Structural mechanism of muscle contraction, Annu. Rev. Biochem. 68, 687-728.
2. Urbanke, C., and Wray, J. (2001) A fluorescence temperature-jump study of conformational transitions in myosin subfragment 1, Biochem. J. 358, 165-173.
3. Málnási-Csizmadia, A., Pearson, D. S., Kovács, M., Woolley, R. J., Geeves, M. A., and Bagshaw, C. R. (2001) Kinetic resolution of a conformational transition and the ATP hydrolysis step using relaxation methods with a Dictyostelium myosin II mutant containing a single tryptophan residue, Biochemistry 40, 12727-12737.
4. Geeves, M. A., and Holmes, K. C. (2005) The molecular mechanism of muscle contraction, Adv. Protein Chem. 71, 161-193.
5. Lymn, R. W., and Taylor, E. W. (1971) Mechanism of adenosine triphosphate hydrolysis by actomyosin, Biochemistry 10, 4617-4624.
6. Mishenina, G. F., Samukov, V. V., and Shubina, T. N. (1979) Selective modification of monosubstituted phosphate groups in nucleoside and oligonucleotide 5′mono- and polyphosphates, Bioorg. Khim. 5, 886-894.
7. Wray, J., and Jahn, W. (2002) γ-amido ATP stabilizes a high fluorescence state of myosin subfragment 1, FEBS Lett. 518, 97-100.
8. Woodward, S. K. A., Eccleston, J. F., and Geeves, M. A. (1991) Kinetics of the interaction of 2′(3′)-O-(N-methylanthraniloyl)- ATP with myosin subfragment 1 and actomyosin subfragment 1: Characterization of two Acto•S1•ADP complexes, Biochemistry 30, 422-430.
9. Hiratsuka, T. (1983) New ribose-modified fluorescent analogs of adenine and guanine nucleotides available as substrates for various enzymes, Biochim. Biophys. Acta 742, 496-508.
10. Málnási-Csizmadia, A., Woolley, R. J., and Bagshaw, C. R. (2000) Resolution of conformational states of dictyostelium myosin II motor domain using tryptophan (W501) mutants: Implications for the open-closed transition identified by crystallography, Biochemistry 39, 16135-16146.
11. Geeves, M. A. (1989) Dynamic interaction between actin and myosin subfragment1 in the presence of ADP, Biochemistry 28, 5864-5871.
12. Siemankowski, R. F., and White, H. D. (1984) Kinetics of the interaction between actin, ADP and cardiac myosin-S1, J. Biol. Chem. 259, 5045-5053.
13. Conibear, P. B. (1999) Kinetic studies on effects of ADP and ionic strength on the interaction between myosin subfragment-1 and actin: Implications for load-sensitivity and regulation of the crossbridge cycle, J. Muscle Res. Cell Motil. 20, 727-742.
14. Kurzawa, S. E., and Geeves, M. A. (1996) A novel stopped flow method for measuring the affinity of actin for myosin head fragments using microgram quantities of protein, J. Muscle Res. Cell Motil. 17, 669-676.
15. Criddle, H., Geeves, M. A., and Jeffries, T. (1985) The use of actin labelled with N-(1-pyrenyl)iodoacetamide to study the interaction of actin with myosin subfragments and troponin/tropomyosin, Biochem. J. 232, 343-349.
16. Ando, T., and Scales, D. (1985) Skeletal muscle myosin subfragment-1 induces bundle formation by actin filaments, J. Biol. Chem. 260, 2321-2327.
17. Blanchoin, L., Didry, D., Carlier, M.-F., and Pantaloni, D. (1996) Kinetics of association of myosin subfragment-1 to unlabeled and pyrenyl-labeled actin, J. Biol. Chem. 271, 12380-12386.
18. 2 cross-linking, Biochemistry 29, 3309-3319.
19. White, H. D., Belknap, B., and Webb, M. R. (1997) Kinetics of nucleoside triphosphate cleavage and phosphate release steps by associated rabbit skeletal actomyosin, measured using a novel fluorescent probe for phosphate, Biochemistry 36, 11828-11836.
20. Smith, D. A., and Geeves, M. A. (1995) Strain-dependent cross-bridge cycle for muscle, Biophys. J. 69, 524-537.
21. Konrad, M., and Goody, R. (1982) Kinetic and thermodynamic properties of the ternary complex between F-actin, myosin subfragment 1 and adenosine 5′-[β,γ-imido]triphosphate, Eur. J. Biochem. 128, 547-555.