Abstract
Using polarization fluorimetry, we have investigated conformational changes of FITC-phalloidin-labeled F-actin in ghost muscle fibers. These changes were induced by myosin subfragment-1 (S1) in the absence and presence of MgADP, MgAMP-PNP, MgATPγS, or MgATP. Modeling of various intermediate states was accompanied by discrete changes in actomyosin orientation and mobility of fluorescent dye dipoles. This suggests multistep changes of orientation and mobility of actin monomers during the ATPase cycle. The most pronounced differences in orientation (∼4°) and in mobility (∼43%) of actin were found between the actomyosin states induced by MgADP and MgATP.
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Abbreviations
- AM:
-
actomyosin
- DTT:
-
dithiothreitol
- S1:
-
myosin subfragment-1
- FITC:
-
fluorescin isothiocyanate
- AMP-PNP:
-
5′-adenylylimidodiphosphate
- ATPγS:
-
adenosine 5′-O-(3-thiotriphosphate)
- pPDM:
-
N,N′-p-phenylenedimaleimide
- NEM:
-
N-ethylmaleimide
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Translated from Biokhimiya, Vol. 70, No. 10, 2005, pp. 1376–1381.
Original Russian Text Copyright © 2005 by Khaimina, Wrzosek, Dabrowska, Borovikov.
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Khaimina, S.S., Wrzosek, A., Dabrowska, R. et al. Orientation and Mobility of Actin in Different Intermediate States of the ATP Hydrolysis Cycle. Biochemistry (Moscow) 70, 1136–1139 (2005). https://doi.org/10.1007/s10541-005-0236-7
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DOI: https://doi.org/10.1007/s10541-005-0236-7