Binding of SH1 - SH2-modified myosin subfragment-1 to actin

Biochemistry

Volumn 37, Issue 22, 1998, Pages 8048-8053

  Xie, Ling ^a   Schoenberg, Mark ^a  

^a NATIONAL INSTITUTE OF ARTHRITIS AND MUSCULOSKELETAL AND SKIN DISEASES   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; MYOSIN;

ACTIN MYOSIN INTERACTION; ARTICLE; BINDING KINETICS; CONFORMATIONAL TRANSITION; ENZYME ACTIVITY; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN PROTEIN INTERACTION;

ACTINS; ADENOSINE TRIPHOSPHATE; ALKYLATING AGENTS; ANIMALS; KINETICS; MALEIMIDES; MYOSIN SUBFRAGMENTS; PROTEIN BINDING; RABBITS; SULFHYDRYL COMPOUNDS; SULFHYDRYL REAGENTS;

EID: 0032474477     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi980319k     Document Type: Article

References (23)

1. Rayment, I., Rypniewski, W. R., Schmidt-Base, K., Smith, R., Tomchick, D. R., Benning, M. M., Winkelmann, D. A., Wesenberg, G., Holden, H. M. (1993) Three-dimensional structure of myosin subfragment-1: a molecular motor. Science 261, 50-58.
2. Yamaguchi, M., and Sekine, T. (1966) Sulfhydryl groups involved in the active site of myosin A adenosine triphosphatase. I. Specific blocking of the SH group responsible for the inhibitory phase in B phasic response of the catalytic activity. J. Biochem. 59, 24-33.
3. Reisler, E., Burke, M., and Harrington, W. F. (1974) Cooperative role of two sulfhydryl groups in myosin adenosine triphosphatase. Biochemistry 13, 2014-2022.
4. Chaen, S., Shimada, M., and Sugi, H. (1986) Evidence for cooperative interactions of myosin heads with thin filament in the force generation of vertebrate skeletal muscle fibers. J. Biol. Chem. 261, 13632-13636.
5. Ehrlich, A., Barnett, V. A., Chen, H. C., and Schoenberg, M. (1995) The site and stoichiometry of the N-phenylmaleimide reaction with myosin when weakly binding cross-bridges are formed in skinned rabbit psoas fibers. Biochim. Biophvs. Acta 1232, 13-20.
6. Huston, E. E., Grammer, J. C., and Yount, R. G. (1988). Flexibility of the myosin heavy chain: Direct evidence that the region containing SH1 and SH2 can move 10 Å under the influence of nucleotide binding. Biochemistry 27, 8945-8952.
7. Barnett, V. A., Ehrlich, A., and Schoenberg, M. (1992) Formation of ATP-insensitive weakly binding cross-bridges in single rabbit psoas fibers by treatment with phenylmaleimide or para-phenylenedimaleimide. Biophys. J. 61, 358-367.
8. Chalovich, J. M., Greene, L. E., and Eisenberg, E. (1983) Cross-linked myosin subfragment 1: A stable analogue of the subfragment-1•ATP complex. Proc. Natl. Acad. Sci. U.S.A. 80, 4909-4913.
9. Xu, S., Yu, L. C., and Schoenberg, M. (1998) Behavior of N-phenylmaleimide-reacted muscle fibers in magnesium-free rigor solution. Biophys. J. 74, 1110-1114.
10. Weeds, A. G., and Pope, B. (1977) Studies on the chymotryptic digestion of myosin. Effects of divalent cations on proteolytic susceptibility. J. Mol. Biol. 111 (2), 129-157.
11. Lowry, O. H., Rosebrough, N. J., Farr, A. L., and Randall, R. J. (1951) Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193, 265-275.
12. Xie, L., Li, W. X., Barnett, V. A., and Schoenberg, M. (1997) Graphical evaluation of alkylation of myosin's SH1 and SH2: The N-phenylmaleimide reaction. Biophvs. J. 72, 858-865.
13. Wells, J. A., and Yount, R. G. (1979) Active site trapping of nucleotides by cross-linking two sulfhydryls in myosin subfragment 1. Proc. Natl. Acad. Sci. U.S.A. 76, 4966-4970.
14. Roopnarine, O., Hideg, K., and Thomas, D. D. (1993) Saturation transfer electron parametric resonance of an indone-dione spin label. Biophys. J. 63, 1896-1907.
15. Lanzetta, P. A., Alvares, L. J., Reinach, P. S., and Candia, A. O. (1979) An improved assay for nanomole amounts of inorganic phosphate. Anal. Biochem. 100, 95-97.
16. i to cross-linked and non-crosslinked Acto•S-1. J. Biol. Chem. 261, 9793-9800.
17. Marquardt, D. W. (1963) An algorithm for least squares estimation of nonlinear parameters. J. Soc. Ind. Appl. Math. 2, 431-441.
18. Marston, S., and Weber, A. (1975) The dissociation constant of the actin-heavy meromyosin subfragment-1 complex. Biochemistry 14, 3868-3873.
19. White, H. D., and Taylor, E. W. (1976) Energetics and mechanism of actomyosin adenosine triphosphatase. Biochemistry 15, 5818-5826.
20. Reisler, E., Burke, M., Himmelfarb, S., and Harrington, W. F. (1974) Spatial proximity of the two essential sulfhydryl groups of myosin. Biochemistry 13, 3837-3840.
21. Botts, J., Thomason, J. F., and Morales, M. F. (1989) On the origin and transmission of force in actomyosin subfragment 1. Proc. Natl. Acad. Sci. U.S.A. 86, 2204-2208.
22. Burke, M., Reisler, E., and Harrington, W. F. (1976) Effect of bridging the two essential thiols of myosin on its spectral and actin-binding properties. Biochemistry 15, 1923-1927.
23. Trentham, D. R., Eccleston, J. F., and Bagshaw, C. R. (1976) Kinetic analysis of ATPase mechanisms. Q. Rev. Biophys. 9, 217-281.