Literature DB >> 11583836

On the elastic properties of tetramethylrhodamine F-actin.

O Cintio1, R Adami, D Choquet, E Grazi.   

Abstract

(Iodoacetamido)tetramethylrhodamine disrupts F-actin. At the 1:1 fluorophore to actin (as monomer) ratio approximately 80% of the protein becomes non-sedimentable. The fluorescent, non-sedimentable actin copolymerizes with G-actin to yield fluorescent filaments. The tensile strength of these filaments changes with the ratio of the fluorescent non-sedimentable actin to the G-actin, being 1.6 pN, 2.9 pN and 3.6 pN at the 1/4, 2/3 and 1/1 ratios, respectively. These tensile strengths are approximately two orders of magnitude lower than those obtained by decoration of F-actin with phalloidin.

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Year:  2001        PMID: 11583836     DOI: 10.1016/s0301-4622(01)00198-3

Source DB:  PubMed          Journal:  Biophys Chem        ISSN: 0301-4622            Impact factor:   2.352


  3 in total

1.  On the mechanics of the actin filament: the linear relationship between stiffness and yield strength allows estimation of the yield strength of thin filament in vivo.

Authors:  Enrico Grazi; Orietta Cintio; Giorgio Trombetta
Journal:  J Muscle Res Cell Motil       Date:  2004       Impact factor: 2.698

2.  Real-time measurements of actin filament polymerization by total internal reflection fluorescence microscopy.

Authors:  Jeffrey R Kuhn; Thomas D Pollard
Journal:  Biophys J       Date:  2004-11-19       Impact factor: 4.033

3.  Formation and destabilization of actin filaments with tetramethylrhodamine-modified actin.

Authors:  Dmitry S Kudryashov; Martin Phillips; Emil Reisler
Journal:  Biophys J       Date:  2004-08       Impact factor: 4.033

  3 in total

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