DOI: 10.1073/pnas.2001892117
论文题名: Muscle myosins form folded monomers; dimers; and tetramers during filament polymerization in vitro
作者: Liu X. ; Shu S. ; Korn E.D.
刊名: Proceedings of the National Academy of Sciences of the United States of America
ISSN: 0027-8424
出版年: 2020
卷: 117, 期: 27 起始页码: 15666
结束页码: 15672
语种: 英语
英文关键词: Electron microscopy
; Muscle myosins
; Polymerization
Scopus关键词: dimer
; monomer
; myosin
; myosin II
; tetramer
; myosin
; myosin II
; animal tissue
; Article
; cardiac muscle
; chicken
; depolymerization
; electron microscopy
; electrophoresis
; gizzard
; in vitro study
; light scattering
; nonhuman
; polymerization
; priority journal
; protein interaction
; skeletal muscle
; smooth muscle
; actin filament
; animal
; chemistry
; genetics
; phosphorylation
; polymerization
; protein conformation
; protein folding
; protein multimerization
; protein unfolding
; ultrastructure
; Actin Cytoskeleton
; Animals
; Chickens
; Microscopy, Electron
; Myosin Type II
; Myosins
; Phosphorylation
; Polymerization
; Protein Conformation
; Protein Folding
; Protein Multimerization
; Protein Unfolding
; Smooth Muscle Myosins
英文摘要: Muscle contraction depends on the cyclical interaction of myosin and actin filaments. Therefore, it is important to understand the mechanisms of polymerization and depolymerization of muscle myosins. Muscle myosin 2 monomers exist in two states: one with a folded tail that interacts with the heads (10S) and one with an unfolded tail (6S). It has been thought that only unfolded monomers assemble into bipolar and side-polar (smooth muscle myosin) filaments. We now show by electron microscopy that, after 4 s of polymerization in vitro in both the presence (smooth muscle myosin) and absence of ATP, skeletal, cardiac, and smooth muscle myosins form tail-folded monomers without tail–head interaction, tail-folded antiparallel dimers, tail-folded antiparallel tetramers, unfolded bipolar tetramers, and small filaments. After 4 h, the myosins form thick bipolar and, for smooth muscle myosin, side-polar filaments. Nonphosphorylated smooth muscle myosin polymerizes in the presence of ATP but with a higher critical concentration than in the absence of ATP and forms only bipolar filaments with bare zones. Partial depolymerization in vitro of nonphosphorylated smooth muscle myosin filaments by the addition of MgATP is the reverse of polymerization. © 2020 National Academy of Sciences. All rights reserved. Citation statistics:
资源类型: 期刊论文
标识符: http://119.78.100.158/handle/2HF3EXSE/163440
Appears in Collections: 气候变化与战略
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作者单位: Liu, X., Laboratory of Cell Biology, Cell and Developmental Biology Center, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892, United States; Shu, S., Laboratory of Cell Biology, Cell and Developmental Biology Center, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892, United States; Korn, E.D., Laboratory of Cell Biology, Cell and Developmental Biology Center, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892, United States
Recommended Citation:
Liu X.,Shu S.,Korn E.D.. Muscle myosins form folded monomers; dimers; and tetramers during filament polymerization in vitro[J]. Proceedings of the National Academy of Sciences of the United States of America,2020-01-01,117(27)