Reindl, Theresia, Giese, Sven, Greve, Johannes N., Reinke, Patrick Y., Chizhov, Igor, Latham, Sharissa L., Mulvihill, Daniel P., Taft, Manuel H., Manstein, Dietmar J. (2022) Distinct actin–tropomyosin cofilament populations drive the functional diversification of cytoskeletal myosin motor complexes. iScience, . ISSN 2589-0042. (doi:10.1016/j.isci.2022.104484) (KAR id:95379)
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Language: English DOI for this version: 10.1016/j.isci.2022.104484
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Official URL: https://doi.org/10.1016/j.isci.2022.104484 |
Abstract
The effects of N-terminal acetylation of the high molecular weight tropomyosin isoforms Tpm1.6 and Tpm2.1 and the low molecular weight isoforms Tpm1.12, Tpm3.1 and Tpm4.2 on the actin affinity and the thermal stability of actin-tropomyosin cofilaments are described. Furthermore, we show how the exchange of cytoskeletal tropomyosin isoforms and their N-terminal acetylation affects the kinetic and chemomechanical properties of cytoskeletal actin-tropomyosin-myosin complexes. Our results reveal the extent to which the different actin-tropomyosin-myosin complexes differ in their kinetic and functional properties. The maximum sliding velocity of the actin filament as well as the optimal motor density for continuous unidirectional movement, parameters that were previously considered to be unique and invariant properties of each myosin isoform, are shown to be influenced by the exchange of the tropomyosin isoform and the N-terminal acetylation of tropomyosin.
Item Type: | Article |
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DOI/Identification number: | 10.1016/j.isci.2022.104484 |
Subjects: |
Q Science > QH Natural history > QH301 Biology Q Science > QH Natural history > QH581.2 Cell Biology Q Science > QP Physiology (Living systems) > QP506 Molecular biology Q Science > QP Physiology (Living systems) > QP517 Biochemistry |
Divisions: | Divisions > Division of Natural Sciences > Biosciences |
Depositing User: | Daniel Mulvihill |
Date Deposited: | 10 Jun 2022 12:21 UTC |
Last Modified: | 13 Jun 2022 08:26 UTC |
Resource URI: | https://kar.kent.ac.uk/id/eprint/95379 (The current URI for this page, for reference purposes) |
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