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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Official URL: 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 |
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DOI/Identification number: | 10.1074/jcb.M100524200 |
Subjects: | Q Science |
Divisions: | Divisions > Division of Natural Sciences > Biosciences |
Depositing User: | Susan Davies |
Date Deposited: | 19 Dec 2007 17:45 UTC |
Last Modified: | 16 Nov 2021 09:38 UTC |
Resource URI: | https://kar.kent.ac.uk/id/eprint/24 (The current URI for this page, for reference purposes) |
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