Abstract
Myosin subfragment 1 (S-1) with its two reactive cysteine groups crosslinked by N,N'-p-phenylenedimaleimide (pPDM), is shown to be a stable analogue of S-1 X ATP and S-1 X ADP X Pi, the predominant complexes present during the steady-state hydrolysis of ATP by S-1. pPDM-S-1 binds to actin with about twice the affinity of S-1 X ATP or S-1 X ADP X Pi, whereas its affinity is 1/100th of that of S-1 X 5'-adenylyl imidodiphosphate and 1/1,000th of that of S-1 X ADP. pPDM-S-1 is also similar to S-1 X ATP and S-1 X ADP X Pi in that its binding to actin is not inhibited by troponin-tropomyosin. In contrast, the binding of S-1, S-1 X ADP, and S-1 X 5'-adenylyl imidodiphosphate to actin is markedly inhibited by troponin-tropomyosin in the absence of Ca2+ when actin is in large excess over S-1. This suggests that modifying S-1 with pPDM stabilizes a conformation which mimics that induced by the binding of ATP.
Full text
PDF




Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Brenner B., Schoenberg M., Chalovich J. M., Greene L. E., Eisenberg E. Evidence for cross-bridge attachment in relaxed muscle at low ionic strength. Proc Natl Acad Sci U S A. 1982 Dec;79(23):7288–7291. doi: 10.1073/pnas.79.23.7288. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Burke M., Reisler F., Harrington W. F. Effect of bridging the two essential thiols of myosin on its spectral and actin-binding properties. Biochemistry. 1976 May 4;15(9):1923–1927. doi: 10.1021/bi00654a020. [DOI] [PubMed] [Google Scholar]
- Chalovich J. M., Chock P. B., Eisenberg E. Mechanism of action of troponin . tropomyosin. Inhibition of actomyosin ATPase activity without inhibition of myosin binding to actin. J Biol Chem. 1981 Jan 25;256(2):575–578. [PMC free article] [PubMed] [Google Scholar]
- Chalovich J. M., Eisenberg E. Inhibition of actomyosin ATPase activity by troponin-tropomyosin without blocking the binding of myosin to actin. J Biol Chem. 1982 Mar 10;257(5):2432–2437. [PMC free article] [PubMed] [Google Scholar]
- Eisenberg E., Greene L. E. The relation of muscle biochemistry to muscle physiology. Annu Rev Physiol. 1980;42:293–309. doi: 10.1146/annurev.ph.42.030180.001453. [DOI] [PubMed] [Google Scholar]
- Eisenberg E., Hill T. L. A cross-bridge model of muscle contraction. Prog Biophys Mol Biol. 1978;33(1):55–82. doi: 10.1016/0079-6107(79)90025-7. [DOI] [PubMed] [Google Scholar]
- Eisenberg E., Kielley W. W. Troponin-tropomyosin complex. Column chromatographic separation and activity of the three, active troponin components with and without tropomyosin present. J Biol Chem. 1974 Aug 10;249(15):4742–4748. [PubMed] [Google Scholar]
- Greene L. E., Eisenberg E. Cooperative binding of myosin subfragment-1 to the actin-troponin-tropomyosin complex. Proc Natl Acad Sci U S A. 1980 May;77(5):2616–2620. doi: 10.1073/pnas.77.5.2616. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Greene L. E., Eisenberg E. Dissociation of the actin.subfragment 1 complex by adenyl-5'-yl imidodiphosphate, ADP, and PPi. J Biol Chem. 1980 Jan 25;255(2):543–548. [PubMed] [Google Scholar]
- Greene L. E., Eisenberg E. The binding of heavy meromyosin to F-actin. J Biol Chem. 1980 Jan 25;255(2):549–554. [PubMed] [Google Scholar]
- Greene L. E., Sellers J. R., Eisenberg E., Adelstein R. S. Binding of gizzard smooth muscle myosin subfragment 1 to actin in the presence and absence of adenosine 5'-triphosphate. Biochemistry. 1983 Feb 1;22(3):530–535. doi: 10.1021/bi00272a002. [DOI] [PubMed] [Google Scholar]
- Greene L. The effect of nucleotide on the binding of myosin subfragment 1 to regulated actin. J Biol Chem. 1982 Dec 10;257(23):13993–13999. [PubMed] [Google Scholar]
- Hill T. L., Eisenberg E., Greene L. Theoretical model for the cooperative equilibrium binding of myosin subfragment 1 to the actin-troponin-tropomyosin complex. Proc Natl Acad Sci U S A. 1980 Jun;77(6):3186–3190. doi: 10.1073/pnas.77.6.3186. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Huxley A. F., Simmons R. M. Proposed mechanism of force generation in striated muscle. Nature. 1971 Oct 22;233(5321):533–538. doi: 10.1038/233533a0. [DOI] [PubMed] [Google Scholar]
- Huxley H. E. The mechanism of muscular contraction. Science. 1969 Jun 20;164(3886):1356–1365. doi: 10.1126/science.164.3886.1356. [DOI] [PubMed] [Google Scholar]
- Moore P. B., Huxley H. E., DeRosier D. J. Three-dimensional reconstruction of F-actin, thin filaments and decorated thin filaments. J Mol Biol. 1970 Jun 14;50(2):279–295. doi: 10.1016/0022-2836(70)90192-0. [DOI] [PubMed] [Google Scholar]
- Parry D. A., Squire J. M. Structural role of tropomyosin in muscle regulation: analysis of the x-ray diffraction patterns from relaxed and contracting muscles. J Mol Biol. 1973 Mar 25;75(1):33–55. doi: 10.1016/0022-2836(73)90527-5. [DOI] [PubMed] [Google Scholar]
- Reedy M. K., Holmes K. C., Tregear R. T. Induced changes in orientation of the cross-bridges of glycerinated insect flight muscle. Nature. 1965 Sep 18;207(5003):1276–1280. doi: 10.1038/2071276a0. [DOI] [PubMed] [Google Scholar]
- Reisler E., Burke M., Himmelfarb S., Harrington W. F. Spatial proximity of the two essential sulfhydryl groups of myosin. Biochemistry. 1974 Sep 10;13(19):3837–3840. doi: 10.1021/bi00716a001. [DOI] [PubMed] [Google Scholar]
- Stein L. A., Schwarz R. P., Jr, Chock P. B., Eisenberg E. Mechanism of actomyosin adenosine triphosphatase. Evidence that adenosine 5'-triphosphate hydrolysis can occur without dissociation of the actomyosin complex. Biochemistry. 1979 Sep 4;18(18):3895–3909. doi: 10.1021/bi00585a009. [DOI] [PubMed] [Google Scholar]
- Wells J. A., Yount R. G. Active site trapping of nucleotides by crosslinking two sulfhydryls in myosin subfragment 1. Proc Natl Acad Sci U S A. 1979 Oct;76(10):4966–4970. doi: 10.1073/pnas.76.10.4966. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Wells J. A., Yount R. G. Chemical modification of myosin by active-site trapping of metal-nucleotides with thiol crosslinking reagents. Methods Enzymol. 1982;85(Pt B):93–116. doi: 10.1016/0076-6879(82)85013-1. [DOI] [PubMed] [Google Scholar]