ADP binding induces an asymmetry between the heads of unphosphorylated myosin.

Berger, C.E.M. and Fagnant, P.M. and Heizmann, S. and Trybus, K.M. and Geeves, M.A. (2001) ADP binding induces an asymmetry between the heads of unphosphorylated myosin. Journal of Biological Chemistry, 276 (26). pp. 23240-23245. (Access to this publication is restricted)

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Abstract

Light chain phosphorylation is the key event that regulates smooth and non-muscle myosin II ATPase activity. Here we show that both heads of smooth muscle heavy meromyosin (HMM) bind tightly to actin in the absence of nucleotide, irrespective of the state of light chain phosphorylation. In striking contrast, only one of the two heads of unphosphorylated HMM binds to actin in the presence of ADP, and the heads have different affinities for ADP. This asymmetry suggests that phosphorylation alters the mechanical coupling between the heads of HMM. A model that incorporates strain between the two heads is proposed to explain the data, which have implications for how one head of a motor protein can gate the response of the other.

Item Type: Article
Subjects: Q Science
Divisions: Faculties > Science Technology and Medical Studies > School of Biosciences > Protein Science Group
Depositing User: Sue Davies
Date Deposited: 19 Dec 2007 17:45
Last Modified: 02 Apr 2014 13:44
Resource URI: http://kar.kent.ac.uk/id/eprint/24 (The current URI for this page, for reference purposes)
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