Equilibrium self-association of tropomyosin
► Skeletal muscle tropomyosin is in equilibrium between monomer, dimer and tetramer. ► Tropomyosin species type determines tropomyosin-actin binding kinetics. ► Analytical ultracentrifugation is an ideal technique to address tropomyosin dynamics. It has recently been reported that tropomyosin exists...
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| Published in | FEBS letters Vol. 586; no. 21; pp. 3840 - 3842 |
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| Main Authors | , , |
| Format | Journal Article |
| Language | English |
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England
Elsevier B.V
02.11.2012
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| Abstract | ► Skeletal muscle tropomyosin is in equilibrium between monomer, dimer and tetramer. ► Tropomyosin species type determines tropomyosin-actin binding kinetics. ► Analytical ultracentrifugation is an ideal technique to address tropomyosin dynamics.
It has recently been reported that tropomyosin exists exclusively as a dimer in physiological salt conditions. It is shown in the present work using analytical ultracentrifugation that, on the contrary, tropomyosin is in equilibrium between monomer, dimer and tetramer with a weak tendency to dimerize and tetramerize. Such a finding has consequences for the assembly of the tropomyosin–actin complex. |
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| AbstractList | It has recently been reported that tropomyosin exists exclusively as a dimer in physiological salt conditions. It is shown in the present work using analytical ultracentrifugation that, on the contrary, tropomyosin is in equilibrium between monomer, dimer and tetramer with a weak tendency to dimerize and tetramerize. Such a finding has consequences for the assembly of the tropomyosin–actin complex.
► Skeletal muscle tropomyosin is in equilibrium between monomer, dimer and tetramer. ► Tropomyosin species type determines tropomyosin‐actin binding kinetics. ► Analytical ultracentrifugation is an ideal technique to address tropomyosin dynamics. It has recently been reported that tropomyosin exists exclusively as a dimer in physiological salt conditions. It is shown in the present work using analytical ultracentrifugation that, on the contrary, tropomyosin is in equilibrium between monomer, dimer and tetramer with a weak tendency to dimerize and tetramerize. Such a finding has consequences for the assembly of the tropomyosin-actin complex. ► Skeletal muscle tropomyosin is in equilibrium between monomer, dimer and tetramer. ► Tropomyosin species type determines tropomyosin-actin binding kinetics. ► Analytical ultracentrifugation is an ideal technique to address tropomyosin dynamics. It has recently been reported that tropomyosin exists exclusively as a dimer in physiological salt conditions. It is shown in the present work using analytical ultracentrifugation that, on the contrary, tropomyosin is in equilibrium between monomer, dimer and tetramer with a weak tendency to dimerize and tetramerize. Such a finding has consequences for the assembly of the tropomyosin–actin complex. |
| Author | Graceffa, Philip Lee, Eunhee Stafford, Walter F. |
| Author_xml | – sequence: 1 givenname: Walter F. surname: Stafford fullname: Stafford, Walter F. – sequence: 2 givenname: Eunhee surname: Lee fullname: Lee, Eunhee – sequence: 3 givenname: Philip surname: Graceffa fullname: Graceffa, Philip email: Graceffa@bbri.org |
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| Copyright | 2012 Federation of European Biochemical Societies FEBS Letters 586 (2012) 2211-5463 ©2015 The Authors. Published by FEBS Press and John Wiley & Sons Ltd. Copyright © 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. 2012 |
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| Keywords | Muscle Analytical ultracentrifugation Tropomyosin Actin |
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Chem. – volume: 33 start-page: 10185 year: 1994 end-page: 10190 article-title: Effects of molecular crowding on protein self-association: a potential source of error in sedimentation coefficients obtained by zonal ultracentrifugation in a sucrose gradient publication-title: Biochemistry – volume: 130 start-page: 89 year: 2007 end-page: 92 article-title: Reconsideration of sedimentation equilibrium distributions reflecting the effects of small inert cosolutes on the dimerization of alpha-chymotrypsin publication-title: Biophys. Chem. – volume: 88 start-page: 1 year: 2008 end-page: 35 article-title: Tropomyosin-based regulation of the actin cytoskeleton in time and space publication-title: Physiol. Rev. – volume: 131 start-page: 839 year: 1979 end-page: 853 article-title: Equilibrium of the actin-tropomyosin interaction publication-title: J. Mol. Biol. – volume: 31 start-page: 287 year: 1988 end-page: 294 article-title: Effect of sucrose on the dimerization of alpha-chymotrypsin. Allowance for thermodynamic nonideality arising from the presence of a small inert solute publication-title: Biophys. Chem. – volume: 47 start-page: 411 year: 1969 end-page: 414 article-title: Physicochemical studies on the aggregation of bovine cardiac tropomyosin with ionic strength publication-title: Can. J. Biochem. – volume: 118 start-page: 209 year: 1978 end-page: 226 article-title: Effects of an intrerchain disulfide bond on tropomyosin structure: intrinsic fluorescence and circular dichroism studies publication-title: J. Mol. Biol. – volume: 43 start-page: 282 year: 1948 end-page: 287 article-title: An X-ray and electron microscope study of tropomyosin publication-title: Biochem. J. – volume: 49 start-page: 27 year: 1951 end-page: 36 article-title: The size, shape and aggregation of tropomyosin particles publication-title: Biochem. J. – volume: 168 start-page: 123 year: 1983 end-page: 141 article-title: Quantitative determination of myosin and actin in rabbit skeletal muscle publication-title: J. Mol. Biol. – volume: 6 start-page: 96 year: 1994 end-page: 104 article-title: Functional properties of non-muscle tropomyosin isoforms publication-title: Curr. Opin. Cell Biol. – volume: 246 start-page: 4226 year: 1971 end-page: 4233 article-title: Reconstitution of troponin activity from three protein components publication-title: J. Biol. Chem. – volume: 41 start-page: 87 year: 1969 end-page: 107 article-title: Tropomyosin: crystal structure, polymorphism and molecular interactions publication-title: J. Mol. Biol. – volume: 67 start-page: 599 year: 2010 end-page: 607 article-title: Tropomyosin is a tetramer under physiological salt conditions publication-title: Cytoskeleton (Hoboken) – volume: 12 year: 2002 article-title: Actin dynamics: tropomyosin provides stability publication-title: Curr. Biol. – volume: 162 start-page: 436 year: 1974 end-page: 441 article-title: The content of troponin, tropomyosin, actin, and myosin in rabbit skeletal muscle myofibrils publication-title: Arch. Biochem. Biophys. – volume: 112 start-page: 346 year: 1966 end-page: 362 article-title: Determination of molecular weights and frictional ratios of proteins in impure systems by use of gel filtration and density gradient centrifugation. Application to crude preparations of sulfite and hydroxylamine reductases publication-title: Biochim. Biophys. Acta. – volume: 43 start-page: 271 year: 1948 end-page: 279 article-title: Tropomyosin: a new asymmetric protein component of the muscle fibril publication-title: Biochem. J. – volume: 108 start-page: 231 year: 2004 end-page: 243 article-title: Analysis of heterologous interacting systems by sedimentation velocity: curve fitting algorithms for estimation of sedimentation coefficients, equilibrium and kinetic constants publication-title: Biophys. 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| Snippet | ► Skeletal muscle tropomyosin is in equilibrium between monomer, dimer and tetramer. ► Tropomyosin species type determines tropomyosin-actin binding kinetics.... It has recently been reported that tropomyosin exists exclusively as a dimer in physiological salt conditions. It is shown in the present work using analytical... |
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| SubjectTerms | Actin Analytical ultracentrifugation Animals Hydrogen-Ion Concentration Kinetics Muscle Polymerization Protein Binding Rabbits Solutions Temperature Thermodynamics Tropomyosin Tropomyosin - chemistry Ultracentrifugation |
| Title | Equilibrium self-association of tropomyosin |
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