Effects of Chemical Modification, Tropomyosin, and Myosin Subfragment 1 on the Yield Strength and Critical Concentration of F-Actin†Click to copy article linkArticle link copied!
Abstract
The effects of coupling with tetramethylrhodamine-5-iodoacetamide and of the decoration with tropomyosin and with myosin subfragment 1 on the elastic properties of F-actin filament are investigated. At 22 °C, in 15 mM orthophosphate and 3 mM MgCl2, tetramethylrhodamine F-actin displays a yield strength of 3.69 ± 0.213 pN and an elastic modulus by stretching of 0.91 MPa. Decoration with tropomyosin increases the yield strength of tetramethylrhodamine F-actin to 10.51 ± 0.24 pN and the elastic modulus by stretching to 23−75 MPa. Mixtures of myosin subfragment 1 and tetramethylrhodamine F-actin at the 0.2:1, 0.4:1, 0.6:1, 0.8:1, and 1:1 molar ratios are also studied. Both yield strength and the elastic modulus by stretching are found to increase progressively with the ratio. At the 1:1 molar ratio, the yield strength is 15.81 ± 0.26 pN and the elastic modulus by stretching is 13.45 to 40 MPa. Decoration of tetramethylrhodamine F-actin with both tropomyosin and myosin subfragment 1, at the 1:1 molar ratio with the actin monomer, produces filaments with an yield strength of 22.3 ± 0.48 pN.
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This work was supported by grants of the University of Ferrara and of the Fondazione della Cassa di Risparmio di Ferrara.
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Università di Ferrara.
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Universitè de Bordeaux.
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Corresponding author: Enrico Grazi, Dipartimento di Biochimica e Biologia Molecolare, Università di Ferrara, Via Borsari 46, 44100 Ferrara, Italy. Phone 0039 0532 291421. Fax 0039 0532 202723. E-mail [email protected].
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This article is cited by 8 publications.
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(6)
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(2)
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