Summary
The five possible analogues of ATP and the three possible analogues of ADP which contain single non-bridging sulphur atoms instead of oxygen in the polyphosphate structure have been used as probes of the interaction of nucleotides with myosin and actomyosin. Evidence is presented for the requirement of an α, β, γ-tridentate complex of magnesium and ATP as the substrate for myosin. Of the four possible tridentate MgATP diastereomers, the Δ exo isomer (nomenclature of Cornelius & Cleland, 1978) appears to be the actual substrate.
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Abbreviations
- ATP:
-
Adenosine-5′-O-triphosphate
- ATP(α-S):
-
Adenosine-5′-O-(1-thiotriphosphate)
- ATP(β-S):
-
Adenosine-5′-O-(2-thiotriphosphate)
- ATP(γ-S):
-
Adenosine-5′-O-(3-thiotriphosphate)
- ADP:
-
Adenosine-5′-O-diphosphate
- ADP(α-S):
-
Adenosine-5′-O-(1-thiodiphosphate)
- ADP(β-S):
-
Adenosine-5′-O-(2-thiodiphosphate)
- Enzyme:
-
Myosin ATPase (EC 3.6.1.3)
References
BAGSHAW, C. R., ECCLESTON, J. F., ECKSTEIN, F., GOODY, R. S., GUTFREUND, H. & TRENTHAM, D. R. (1974) The magnesium ion dependent adenosine triphosphatase of myosin.Biochem. J. 141, 351–64.
BAGSHAW, C. R., ECCLESTON, J. F., TRENTHAM, D. R., YATES, D. W. & GOODY, R. S. (1972) Transient kinetic studies of the Mg2+-dependent ATPase of myosin and its proteolytic subfragments.Cold Spring Harb. Symp. quan. Biol. 37, 127–35.
BAGSHAW, C. R. & TRENTHAM, D. R. (1974) The characterization of myosin-product complexes and of product release steps during the Mg++-dependent adenosine triphosphatase reaction.Biochem. J. 141, 331–49.
BARRINGTON LEIGH, J., HOLMES, K. C., MANNHERZ, H. G., ROSENBAUM, G., ECKSTEIN, F. & GOODY, R. S. (1972) Effect of ATP analogs on the low-angle X-ray diffraction pattern of insect flight muscle.Cold Spring Harb. symp. quant. Biol. 37, 443–7.
BURGERS, P. M. & ECKSTEIN, F. (1978) Absolute configuration of the diastereomers of adenosine 5′-0-(1-thiophosphate): Consequences for the stereochemistry of polymerization by DNA-dependent RNA polymerase fromEscherichia coli.Proc. natn. Acad. Sci. U.S.A. 75, 4798–800.
CORNELIUS, R. C. & CLELAND, W. W. (1978) Substrate activity of (adenosine triphosphate) tetraaminecobalt (III) with yeast hexokinase and separation of diastereomers.Biochemistry 17, 3279–86.
DRABIKOWSKI, W. & GERGELY, J. (1963) The role of sulfhydryl groups in the polymerization and adenosine triphosphate binding of G-actin.J. biol. Chem. 238, 640–3.
ECCLESTON, J. F. & TRENTHAM, D. R. (1979) Magnesium ion dependent rabbit muscle myosin guanosine and thioguanosine triphosphatase mechanism and a novel guanosine diphosphatase reaction.Biochemistry 18, 2896–904.
ECKSTEIN, F. & GOODY, R. S. (1976) Synthesis and properties of diastereomers of adenosine 5′-0-(1-thiotriphosphate) and adenosine 5′-0-(2-thiotriphosphate).Biochemistry 15, 1685–91.
ECKSTEIN, F., GOODY, R. S. & TRENTHAM, D. R. (1973) Hydrolyse von Thiophosphatanalogen des ATP durch Myosinfragment S1.Hoppe-Seyler's Z. physiol. Chem. 354, 233–4.
GOODNO, C. C. (1979) Inhibition of myosin ATPase by vanadate ion.Proc. natn. Acad. Sci. U.S.A. 76, 2620–4.
GREENE, L. E. & EISENBERG, E. (1978). Formation of a ternary complex: actin, 5′-adenyl imidodiphosphate and the subfragments of myosin.Proc. natn. Acad. Sci. U.S.A. 75, 54–8.
HOFMANN, W. & GOODY, R. S. (1978) The ternary complex formed between actin, myosin subfragment 1 and ATP(β,γ-NH).FEBS Lett. 89, 169–72.
JAFFE, E. K. & COHN, M. (1978) Divalent cation-dependent stereospecificity of adenosine 5′-0-(2-thiophosphate) in the hexokinase and pyruvate kinase reactions.J. biol. Chem. 253, 4823–5.
JOHNSON, K. A. & TAYLOR, E. W. (1978) Intermediate states of subfragment 1 and actosub-fragment 1 ATPase: re-evaluation of the mechanism.Biochemistry 17, 3432–42.
MANNHERZ, H. G., BARRINGTON LEIGH, J., HOLMES, K. C. & ROSENBAUM, G. (1973) Identification of the transient complex myosin-ATP by the use of α,β-methylene ATP.Nature 241, 226–9.
STAHL, K. W., SCHLIMME, E. & ECKSTEIN, F. (1974) Yeast hexokinase reaction with adenosine 5′-0-triphosphate and adenosine 5′-0-(1-thiotriphosphate) monitored by liquid chromatography.FEBS Lett. 40, 241–6.
TRYBUS, K. M. & TAYLOR, E. W. (1979) Kinetics of ADP and AMP-PNP binding to SF-1.Biophys. J. 25, 21a.
WEEDS, A. G. & TAYLOR, R. S. (1975) Separation of subfragment-1 isoenzymes from rabbit skeletal muscle myosin.Nature 257, 54–6.
WHITE, H. D. (1977) Magnesium-ATP binding to acto-myosin S1 and acto-heavy meromyosin.Biophys. J. 17, 40a.
WHITE, H. D. & TAYLOR, E. W. (1976) Energetics and mechanism of actomyosin adenosine triphosphatase.Biochemistry 15, 5818–28.
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Goody, R.S., Hofmann, W. Stereochemical aspects of the interaction of myosin and actomyosin with nucleotides. J Muscle Res Cell Motil 1, 101–115 (1980). https://doi.org/10.1007/BF00711928
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DOI: https://doi.org/10.1007/BF00711928