Effect of the N-terminal extension in myosin essential light chain A1 on the mechanism of actomyosin ATP hydrolysis.
Autor: | Heeley DH; Department of Biochemistry, Memorial University, St John's, Newfoundland, Canada. Electronic address: dheeley@mun.ca., Belknap B; Department of Physiological Sciences, Eastern Virginia Medical School, Norfolk, Virginia, USA., Atherton JL; Department of Physiological Sciences, Eastern Virginia Medical School, Norfolk, Virginia, USA., Hasan SC; Department of Biochemistry, Memorial University, St John's, Newfoundland, Canada., White HD; Department of Physiological Sciences, Eastern Virginia Medical School, Norfolk, Virginia, USA. |
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Jazyk: | angličtina |
Zdroj: | The Journal of biological chemistry [J Biol Chem] 2024 Jan; Vol. 300 (1), pp. 105521. Date of Electronic Publication: 2023 Dec 01. |
DOI: | 10.1016/j.jbc.2023.105521 |
Abstrakt: | Myosin essential light chains A1 and A2 are identical isoforms except for an extension of ∼40 amino acids at the N terminus of A1 that binds F-actin. The extension has no bearing on the burst hydrolysis rate (M-ATP → M-ADP-Pi) as determined by chemical quench flow (100 μM isoenzyme). Whereas actomyosin-S1A2 steady state MgATPase (low ionic strength, 20 °C) is hyperbolically dependent on concentration: V Competing Interests: Conflict of interest The authors declare that they have no competing interests. (Copyright © 2023 The Authors. Published by Elsevier Inc. All rights reserved.) |
Databáze: | MEDLINE |
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