Actin and temperature effects on the cross-linking of the SH1-SH2 helix in myosin subfragment 1

Biophysical Journal

Volumn 78, Issue 6, 2000, Pages 3072-3080

  Nitao, Lisa K ^a   Reisler, Emil ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATASE; MYOSIN; NUCLEOTIDE; THIOL DERIVATIVE;

ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; CROSS LINKING; DYNAMICS; ENZYME ACTIVITY; NONHUMAN; PROTEIN BINDING; RABBIT; TEMPERATURE;

EID: 0034083446     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(00)76844-5     Document Type: Article

References (38)

1. Aguirre, R., S. H. Lin, F. Gonsoulin, C. K. Wang, and H. C. Cheung. 1989. Characterization of the ethenoadenosine diphosphate binding site of myosin subfragment 1. Energetics of the equilibrium between two states of nucleotide. S1 and vanadate-induced global conformation changes detected by energy transfer. Biochemistry. 28:799-807.
2. Baker, J. E., I. Brust-Mascher, S. Ramachandran, L. E. LaConte, and D. D. Thomas. 1998. A large and distinct rotation of the myosin light chain domain occurs upon muscle contraction. Proc. Natl. Acad. Sci. USA. 95:2944-2949.
3. Batra, R., M. A. Geeves, and D. J. Manstein. 1999. Kinetic analysis of Dictyostelium discoideum myosin motor domain with glycine-to-alanine mutations in the reactive thiol region. Biochemistry. 38:6126-6134.
4. Burke, M., and E. Reisler. 1977. Effect of nucleotide binding on the proximity of the essential sulfhydryl groups of myosin. Chemical probing of movement of residues during conformational transitions. Biochemistry. 16:5559-5563.
5. Cartoux, L., T. Chen, G. DasGupta, P. B. Chase, M. J. Kushmerick, and E. Reisler. 1992. Antibody and peptide probes of interactions between the SH1-SH2 region of myosin subfragment 1 and actin's N-terminus. Biochemistry. 31:10929-10935.
6. Chaussepied, P., D. Mornet, and R. Kassab. 1986. Nucleotide trapping at the ATPase site of myosin subfragment 1 by a new interthiol crosslinking. Proc. Natl. Acad Sci. USA. 83:2037-2041.
7. Cooke, R. 1997. Actomyosin interaction in striated muscle. Physiol. Rev. 77:671-697.
8. Dominguez, R., Y. Freyzon, K. M. Trybus, and C. Cohen. 1998. Crystal structure of a vertebrate smooth muscle myosin motor domain and its complex with the essential light chain: visualization of the pre-power stroke state. Cell. 94:559-571.
9. Duke, J., R. Takashi, K. Ue, and M. F. Morales. 1976. Reciprocal reactivities of specific thiols when actin binds to myosin. Proc. Natl. Acad. Sci. USA. 73:302-306.
10. 4. Biochemistry. 34:8960-8972.
11. Fiske, C. H., and Y. Subbarow. 1925. The colorimetric determination of phosphorus. J. Biol. Chem. 60:375-400.
12. Godfrey, J. E., and W. F. Harrington. 1970. Self-association in the myosin system at high ionic strength. I. Sensitivity of the interaction to pH and ionic environment. Biochemistry. 9:886-893.
13. Gulick, A. M., C. B. Bauer, J. B. Thoden, and I. Rayment. 1997. X-ray structures of the MgADP, MgATPγS, and MgAMPPNP complexes of the Dictyostelium discoideum myosin motor domain. Biochemistry. 36: 11619-11628.
14. Highsmith, S., and O. Jardetzky. 1980. G-actin binding quenches internal motions in myosin subfragment-1. FEBS Lett. 121:55-60.
15. Hiratsuka, Y., M. Eto, M. Yazawa, and F. Morita. 1998. Reactivities of Cys707 (SH1) in intermediate states of myosin subfragment-1 ATPase. J. Biochem. 124:609-614.
16. Houdusse, A., V. N. Kalabokis, D. Himmel, A. G. Szent-Gyorgyi, and C. Cohen. 1999. Atomic structure of scallop myosin subfragment S1 complexed with MgADP: a new conformation for the myosin head. Cell. 97:459-470.
17. Kameyama, T., and T. Sekine. 1973. Effect of F-actin on the reactivity of a specific sulfhydryl group (S2) in heavy meromyosin. J. Biochem. 74:1283-1285.
18. Kinose, F., S. X. Wang, U. S. Kidambi, C. L. Moneman, and D. A. Winkelmann. 1996. Glycine 699 is pivotal for the motor activity of skeletal muscle myosin. J. Cell. Biol. 134:895-909.
19. Kliche, W., M. T. Pfannstiel, S. Stoeva, and H. Faulstich. 1999. Thiol-specific cross-linkers of variable length reveal a similar separation of SH1 and SH2 in myosin subfragment 1 in the presence and absence of MgADP. Biochemistry. 38:10307-10317.
20. Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:680-685.
21. 2+ to actin without loss of polymerizability: the involvement of the rapidly reacting -SH group. Arch. Biochem. Biophys. 150:164-174.
22. Miller, C. J., and E. Reisler. 1995. Role of charged amino acid pairs in subdomain-1 of actin in interactions with myosin. Biochemistry. 34: 2694-2700.
23. Moore, P. B., H. E. Huxley, and D. J. DeRosier. 1970. Three-dimensional reconstruction of F-actin, thin filaments and decorated thin filaments. J. Mol. Biol. 50:279-295.
24. Mornet, D., K. Ue, and M. F. Morales. 1985. Stabilization of a primary loop in myosin subfragment 1 with a fluorescent crosslinker. Proc. Natl. Acad. Sci. USA. 82:1658-1662.
25. Nikolaeva, O. P., V. N. Orlov, I. V. Dedova, V. A. Drachev, and D. I. Levitsky. 1996. Interaction of myosin subfragment 1 with F-actin studied by differential scanning calorimetry. Biochem. Mol. Biol. Int. 40: 653-661.
26. Nitao, L. K., and E. Reisler. 1998. Probing the conformational states of the SH1-SH2 helix in myosin: a cross-linking approach. Biochemistry. 37: 16704-16710.
27. Patterson, B., K. M. Ruppel, Y. Wu, and J. A. Spudich. 1997. Cold-sensitive mutants G680V and G691C of Dictyostelium myosin II confer dramatically different biochemical defects. J. Biol. Chem. 272: 27612-27617.
28. Polosukhina, K., and S. Highsmith. 1997. Kinetic investigation of the ligand dependence of rabbit skeletal muscle myosin subfragment 1 Cys-697 and Cys-707 reactivities. Biochemistry. 36:11952-11958.
29. Rayment, I. 1996. The structural basis of the myosin ATPase activity. J. Biol. Chem. 271:15850-15853.
30. Roopnarine, O., A. G. Szent-Györgyi, and D. D. Thomas. 1998. Microsecond rotational dynamics of spin-labeled myosin regulatory light chain induced by relaxation and contraction of scallop muscle. Biochemistry. 37:14428-14436.
31. Schwyter, D., M. Phillips, and E. Reisler. 1989. Subtilisin-cleaved actin: polymerization and interaction with myosin subfragment 1. Biochemistry. 28:5889-5895.
32. Shriver, J. W. 1986. The structure of myosin and its role in energy transduction in muscle. Biochem. Cell Biol. 64:265-276.
33. Spudich, J. A., and S. Watt. 1971. The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin. J. Biol. Chem. 246:4866-4871.
34. Uyeda, T. Q., P. D. Abramson, and J. A. Spudich. 1996. The neck region of the myosin motor domain acts as a lever arm to generate movement. Proc. Natl. Acad. Sci. USA. 93:4459-4464.
35. Walker, M., H. White, B. Belknap, and J. Trinick. 1994. Electron cryomicroscopy of acto-myosin-S1 during steady-state ATP hydrolysis. Biophys. J. 66:1563-1572.
36. Walker, M., X. Z. Zhang, W. Jiang, J. Trinick, and H. D. White. 1999. Observation of transient disorder during myosin subfragment-1 binding to actin by stopped-flow fluorescence and millisecond time resolution electron cryomicroscopy: evidence that the start of the cross-bridge power stroke in muscle has variable geometry. Proc. Natl. Acad. Sci. USA. 96:465-470.
37. Weeds, A. G., and B. Pope. 1977. Studies on the chymotryptic digestion of myosin. Effects of divalent cations on proteolytic susceptibility. J. Mol. Biol. 111:129-157.
38. Wells, J. A., C. Knoeber, M. C. Sheldon, M. M. Werber, and R. G. Yount. 1980. Cross-linking of myosin subfragment 1. Nucleotide-enhanced modification by a variety of bifunctional reagents. J. Biol. Chem. 255: 11135-11140.