The Antiparallel Coiled-Coil Domain Allows Multiple Forward Step Sizes of Myosin X.
J Phys Chem Lett
; 14(21): 4914-4922, 2023 Jun 01.
Article
em En
| MEDLINE
| ID: mdl-37202741
ABSTRACT
Myosin X forms an antiparallel dimer and moves processively on actin bundles. How the antiparallel dimer affects the stepping mechanism of myosin X remains elusive. Here, we generated several chimeras using domains of myosin V and X and performed single-molecule motility assays. We found that the chimera containing the motor domain from myosin V and the lever arm and antiparallel coiled-coil domain from myosin X has multiple forward step sizes and moves processively, similar to full-length myosin X. The chimera containing the motor domain and lever arm from myosin X and the parallel coiled-coil from myosin V takes steps of â¼40 nm at lower ATP concentrations but was nonprocessive at higher ATP concentrations. Furthermore, mutant myosin X with four mutations in the antiparallel coiled-coil domain failed to dimerize and was nonprocessive. These results imply that the antiparallel coiled-coil domain is necessary for multiple forward step sizes of myosin X.
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Base de dados:
MEDLINE
Assunto principal:
Miosina Tipo V
Idioma:
En
Ano de publicação:
2023
Tipo de documento:
Article