Conformational changes of F-actin in myosin-free ghost single fibre induced by either phosphorylated or dephosphorylated heavy meromyosin

Kakol, I; Borovikov, Yurii S.; Szczêsna, Danuta; Kirillina, V P; Levitsky, Dmitrii I.

doi:10.1016/0167-4838(87)90225-1

Cited by 37 publications

(19 citation statements)

References 24 publications

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“…In this model, it is assumed that there are two populations of probes in the fiber: N probes with a disordered orientation and (1 À N) probes with an ordered orientation. The axes of dipoles of the ordered probes are arranged in a spiral along the surface of the cone, the axis of which coincides with the long axis of actin filament [54,55]. The dipoles of fluorescence absorption and emission form the angles U A and U E , respectively, at the top of the cone.…”

Section: Fluorescence Polarization Measurementmentioning

confidence: 99%

Aberrant movement of β-tropomyosin associated with congenital myopathy causes defective response of myosin heads and actin during the ATPase cycle

Borovikov

Avrova

Rysev

et al. 2015

Archives of Biochemistry and Biophysics

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Section: Fluorescence Polarization Measurementmentioning

confidence: 99%

Aberrant movement of β-tropomyosin associated with congenital myopathy causes defective response of myosin heads and actin during the ATPase cycle

Borovikov

Avrova

Rysev

et al. 2015

Archives of Biochemistry and Biophysics

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“…The existence of two states of rigor complexes of F-actin and heavy meromyosin, flexible and rigid, has been postulated [47].…”

Section: The Role Of Light Chains and Their N-terminal Parts In The Mmentioning

confidence: 99%

The role of the skeletal muscle myosin light chains N‐terminal fragments

Stȩpkowski

1995

FEBS Letters

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The myosin regulatory and essential fight chains in skeletal muscle do not play a role as significant as in scallop or smooth muscle, however, there are some data suggesting that the skeletal myosin fight chains and their N-terminal parts may have a modulatory function in the interaction of actin with myosin heads. In this paper four conformational states of the myosin head with respect to the regulatory light chain bound cation (magnesium or calcium) and phosphorylation are proposed. Communication between regulatory and essential light chains and putative binding of the N-terminus of A1 essential light chain to actin is discussed.

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“…For example, flexibility of the actin filament changes when myosin or regulatory proteins bind to actin. 11,22,26,28,[32][33][34]37,42 This suggests that alterations of rotational motions or distortions of actin monomers in the filament, or possibly some slits between the domains occur during force generation. 29 In the present article, the conformation of the thin filament was studied by polarizing spectrofluorimetry.…”

mentioning

confidence: 96%

“…Incorporation of S-1 into the ghost fibers and determination of the molar ratios of S-1 were performed as described earlier. 4,22 Measurements of Polarized Fluorescence. Extrinsic fluorescence of F-actin labeled with rhodaminephalloidin or 1,5-IAEDANS was studied.…”

mentioning

confidence: 99%

“…The conformation of F-actin was studied in single ''ghost'' fibers, as described in detail earlier. 22,35,40,41 Exogenous fluorophores, rhodamine-phalloidin and 1,5-IAEDANS, were used for studying the changes in actin structure in the above-mentioned atrophic muscles. To gain more information regarding the structural arrangement of the actin filament, the effect of myosin subfragment-1 (S-1) on the actin conformation was also investigated.…”

mentioning

confidence: 99%

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