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- Title
Suggesting Dictyostelium as a Model for Disease-Related Protein Studies through Myosin II Polymerization Pathway.
- Authors
Liu, Xiong; Shu, Shi
- Abstract
Dictyostelium myosin II displays remarkable dynamism within the cell, continually undergoing polymerization and depolymerization processes. Under low-ion conditions, it assumes a folded structure like muscle myosins and forms thick filaments through polymerization. In our study, we presented intermediate structures observed during the early stages of polymerization of purified myosin via negative staining electron microscopy, immediately crosslinked with glutaraldehyde at the onset of polymerization. We identified folded monomers, dimers, and tetramers in the process. Our findings suggest that Dictyostelium myosin II follows a polymerization pathway in vitro akin to muscle myosin, with folded monomers forming folded parallel and antiparallel dimers that subsequently associate to create folded tetramers. These folded tetramers eventually unfold and associate with other tetramers to produce long filaments. Furthermore, our research revealed that ATP influences filament size, reducing it regardless of the status of RLC phosphorylation while significantly increasing the critical polymerization concentrations from 0.2 to 9 nM. In addition, we demonstrate the morphology of fully matured Dictyostelium myosin II filaments.
- Subjects
MYOSIN; DICTYOSTELIUM; POLYMERIZATION; PROTEIN models; ELECTRON microscopy; DEPOLYMERIZATION
- Publication
Cells (2073-4409), 2024, Vol 13, Issue 3, p263
- ISSN
2073-4409
- Publication type
Article
- DOI
10.3390/cells13030263