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The myosin ATPase mechanism does not require a conformationally sensitive aromatic residue

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Summary

The effect of nucleotides or calcium ([Ca2+]free=1.0×10−4 m) or both on the near-u.v. absorption spectrum of myosins purified from two species of scallop,Aequipecten irradians andPlacopecten magellanicus, has been examined. No change in tyrosyl or tryptophanyl absorption was detected.

The near-ultraviolet (u.v.) circular dichroism (CD) spectra of myosins from these two species of scallop were examined on a high sensitivity (Jasco J41C) spectropolarimeter.Aequipecten andPlacopecten myosin near-u.v. CD spectra were qualitatively distinct. The near-u.v. CD spectrum ofPlacopecten myosin was not perturbed by addition of a ten-fold molar excess of ADP±Ca2+, 0.1m PPi or 1.0×10−4 m calcium alone. ADP and PPi did induce small, qualitatively distinct changes in the near-u.v. CD spectrum ofAequipecten myosin but no perturbation was observed with calcium alone.

These data, together with those from an earlier study, indicate that the conformation of aromatic residues are not necessarily perturbed in the myosin ATPase mechanism as has previously been suggested.

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References

  • BAGSHAW, C. R., ECCLESTON, J. F., ECKSTEIN, F., GOODY, R. S., GUTFREUND, H. & TRENTHAM, D. R. (1974) The magnesium ion-dependent triphosphatase of myosin.Biochem. J. 141, 351–64.

    Google Scholar 

  • BAGSHAW, C. R. & TRENTHAM, D. R. (1974) The characterization of myosin-product complexes and of product-release steps during the magnesium ion-dependent adenosine triphosphate reaction.Biochem. J. 141, 331–49.

    Google Scholar 

  • BULLARD, B., MERCOLA, D. A. & MOMMAERTS, W. F. H. M. (1976) The origin of the tyrosyl circular dichroism of tropomyosin.Biochim. Biophys. Acta 434, 90–9.

    Google Scholar 

  • CASSIM, M. Y. & LIN, T. I. (1975) Does myosin-substrate interactionin vitro result in a delocalized conformation change?J. Supra. Struct. 3, 510–9.

    Google Scholar 

  • CHANTLER, P. D., SELLERS, J. R. & SZENT-GYÖRGYI, A. G. (1981) Cooperativity in scallop myosin.Biochemistry 20, 210–6.

    Google Scholar 

  • CHANTLER, P. D. & SZENT-GYÖRGYI, A. G. (1978) Spectroscopic studies on invertebrate myosin and light-chains.Biochemistry 17, 5440–8.

    Google Scholar 

  • CHANTLER, P. D. & SZENT-GYÖRGYI, A. G. (1980) Regulatory light-chains and scallop myosin: full dissociation, reversibility and cooperative effects.J. molec. Biol. 138, 473–92.

    Google Scholar 

  • CHOCK, S. P. (1979) The mechanism of muscle myosin ATPase III.J. biol. Chem. 15, 3244–53.

    Google Scholar 

  • CHOCK, S. P., CHOCK, P. B. & EISENBERG, E. (1976) Pre-steady-state kinetic evidence for a cyclic interaction of myosin subfragment one with actin during the hydrolysis of adenosine 5′-triphosphate.Biochemistry 15, 3244–53.

    Google Scholar 

  • CHOCK, S. P., CHOCK, P. B. & EISENBERG, E. (1979) The mechanism of the skeletal muscle myosin ATPase II.J. biol. Chem. 254, 3236–43.

    Google Scholar 

  • CHOCK, S. P. & EISENBERG, E. (1979) The mechanism of the skeletal muscle myosin ATPase I.J. biol. Chem. 254, 3229–35.

    Google Scholar 

  • ECCLESTON, J. F. & BAYLEY, P. M. (1980) Circular dichroic spectra of 6-thioguanosine nucleotide and their complexes with myosin subfragment-1.Biochemistry 19, 5050–6.

    Google Scholar 

  • FERENCZI, M. A., HOMSHER, E., SIMMONS, R. M. & TRENTHAM, D. R. (1978) Reaction mechanism of the magnesium ion-dependent adenosine triphosphatase of frog muscle myosin and subfragment 1.Biochem. J. 171, 165–75.

    Google Scholar 

  • HORWITZ, J., STICKLAND, E. H. & BILLUPS, C. (1970) Analysis of the vibrational structure in the near-ultraviolet circular dichroism and absorption spectrum of tyrosine derivatives and ribonuclease-A at 77°K.J. Am. chem. Soc. 92, 2119–29.

    Google Scholar 

  • HOUK, T. S. & UE, K. (1974) The measurement of actin concentration in solution: a comparison of methods.Analyt. Biochem. 62, 66–74.

    Google Scholar 

  • JOHNSON, K. A. & TAYLOR, E. W. (1978) Intermediate states of subfragment 1 and actosubfragment 1 ATPase: Reevaluation of the mechanism.Biochemistry 17, 3432–42.

    Google Scholar 

  • KARDAMI, E., DEBRUIN, S. H. & GRATZER, W. B. (1979) Interaction of ADP with skeletal and cardiac myosin and their active fragment observed by proton release.Eur. J. Biochem. 97, 547–53.

    Google Scholar 

  • KENDRICK-JONES, J., LEHMAN, W. & SZENT-GYÖRGYI, A. G. (1970) Regulation in molluscan muscles.J. molec. Biol. 54, 313–26.

    Google Scholar 

  • KENDRICK-JONES, J., SZENTKIRALYI, E. M. & SZENT-GYÖRGYI, A. G. (1976) Regulatory light-chains in myosins.J. molec. Biol. 104, 747–75.

    Google Scholar 

  • KIELY, B. & MARTONOSI, A. (1968) Kinetics and substrate binding of myosin adenosine triphosphatase.J. biol. Chem. 243, 2273–8.

    Google Scholar 

  • KONDO, S., ASAKAWA, T. & MORITA, F. (1979) Difference UV absorption spectrum of scallop adductor muscle myosin induced by ATP.J. Biochemistry 86, 1567–71.

    Google Scholar 

  • LAEMMLI, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4.Nature 227, 680–5.

    Google Scholar 

  • MARSH, D. J., D'ALBIS, A. & GRATZER, W. B. (1978) Optical spectroscopic study of the ADP-myosin interaction.Eur. J. Biochem. 82, 219–24.

    Google Scholar 

  • MARSH, D. J., DEBRUIN, S. H. & GRATZER, W. B. (1977) An investigation of heavy meromyosin-ADP binding equilibrium by proton release measurement.Biochemistry 16, 1738–42.

    Google Scholar 

  • MORITA, F. (1967) Interaction of heavy meromyosin with substrate.J. biol. Chem. 242, 4501–6.

    Google Scholar 

  • MURPHY, A. J. (1974) Circular dichroism of the adenine and 6-mercaptopurine nucleotide complexes of heavy meromyosin.Archs Biochem. Biophys. 163, 290–6.

    Google Scholar 

  • SHIMIZU, T. (1977) Bovine platelet myosin: fluorescence of the tryptophenyl groups.J. Biochemistry 82, 1491–4.

    Google Scholar 

  • SLEEP, J. A. & TAYLOR, E. W. (1976) Intermediate states of actomyosin adenosine triphosphatase.Biochemistry 15, 5813–7.

    Google Scholar 

  • SMITH, S. J. (1979) A circular dichroism study of cardiac myosin and its interaction with ADP.FEBS Lett. 105, 197–200.

    Google Scholar 

  • STRICKLAND, E. H., HORWITZ, J. & BILLUPS, C. (1969) Fine structure in the near-ultraviolet circular dichroism and absorption spectra of tryptophan derivatives and chymotrypsinogen-A at 77°K.Biochemistry 8, 3205–13.

    Google Scholar 

  • SZENT-GYÖRGYI, A. G. (1975) Calcium regulation of muscle contraction.Biophys. J. 15, 707–23.

    Google Scholar 

  • TAUSSKY, H. M. & SCHORR, E. (1952) A microcolorimetric method for the determination of inorganic phosphate.J. biol. Chem. 202, 675–85.

    Google Scholar 

  • WALLIMAN, T. & SZENT-GYÖRGYI, A. G. (1981) An immunological approach to myosin light-chain function in thick filament-linked regulation.Biochemistry 20, 1176–87.

    Google Scholar 

  • WERBER, M. M., SZENT-GYÖRGYI, A. G. & FASMAN, G. D. (1972) Fluorescence studies on heavy meromyosin substrate interactions.Biochemistry 11, 2872–83.

    Google Scholar 

  • WU, C. S. C. & YANG, J. T. (1976) Reexamination of the conformation of muscle proteins by optical activity.Biochemistry 15, 3007–14.

    Google Scholar 

  • YAMADA, T., SHIMIZU, H., NAKANISHI, M. & TSUBOI, M. (1981) Environment of the tryptophan residues in the myosin head: a hydrogen-deuterium exchange study.Biochemistry 20, 1162–8.

    Google Scholar 

  • YOSHIDA, M. & MORITA, F. (1976) A study of the binding of adenosine diphosphate to myosin subfragment-1.J. Biochemistry 79, 1049–52.

    Google Scholar 

  • YOSHINO, H., MORITA, F. & YAGI, K. (1972) The difference absorption spectrum of myosin induced by adenosine triphosphate, adenosine diphosphate and inorganic pyrophosphate.J. Biochemistry 71, 351–3.

    Google Scholar 

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Author notes

  1. David J. Marsh

    Present address: Laboratoire de Neurobiologie, Ecole Normale Supérieur, 46 rue d'Ulm, 75230, Paris Cedex 05, France

Authors and Affiliations

  1. Department of Biology, Brandeis University, 02254, Waltham, Massachusetts, USA

    Peter D. Chantler

  2. Rosenstiel Basic Medical Science Laboratories, Brandeis University, Waltham, Massachusetts, USA

    David J. Marsh

  3. National Institute for Medical Research, Mill Hill, London, UK

    Stephen R. Martin

Authors
  1. Peter D. Chantler
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  2. David J. Marsh
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  3. Stephen R. Martin
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Chantler, P.D., Marsh, D.J. & Martin, S.R. The myosin ATPase mechanism does not require a conformationally sensitive aromatic residue. J Muscle Res Cell Motil 2, 453–466 (1981). https://doi.org/10.1007/BF00711970

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