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

Berger, C.E.M., Fagnant, P.M., Heizmann, S., Trybus, K.M., Geeves, Michael A. (2001) ADP binding induces an asymmetry between the heads of unphosphorylated myosin. Journal of Biological Chemistry, 276 (26). pp. 23240-23245. ISSN 0021-9258. E-ISSN 1083-351X. (doi:10.1074/jcb.M100524200) (Access to this publication is currently restricted. You may be able to access a copy if URLs are provided) (KAR id:24)

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http://dx.doi.org/10.1074/jcb.M100524200

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
DOI/Identification number: 10.1074/jcb.M100524200
Subjects: Q Science
Divisions: Faculties > Sciences > School of Biosciences > Protein Science Group
Depositing User: Susan Davies
Date Deposited: 19 Dec 2007 17:45 UTC
Last Modified: 23 Jan 2020 04:00 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/24 (The current URI for this page, for reference purposes)
Geeves, Michael A.: https://orcid.org/0000-0002-9364-8898
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