Molecular plasticity of the native mouse skeletal sarcomere revealed by cryo-ET
Molecular plasticity of the native mouse skeletal sarcomere revealed by cryo-ET
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冷冻电子断层扫描（cryo-ET）揭示天然小鼠骨骼肌节的分子可塑性
DOI：
10.1101/2020.09.13.295386
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发表时间：
2020
期刊：
影响因子：
--
通讯作者：
Wang Z
中科院分区：
文献类型：
--
作者：
Wang Z
Sarcomeres are the force-generating and load-bearing devices of muscles. A precise molecular understanding of how the entire sarcomere is built is required to understand its role in health, disease and ageing. Here, we determine thein situmolecular architecture of vertebrate skeletal sarcomeres through electron cryo-tomography of cryo-focused ion beam-milled native myofibrils. The reconstructions reveal the three-dimensional organisation and interaction of actin and myosin filaments in the A-band, I-band and Z-disc and demonstrate how α -actinin cross-links antiparallel actin filaments to form a mesh-like structure in the Z-disc at an unprecedented level of molecular detail. A prominent feature is a so-far undescribed doublet of α-actinin cross-links with ∼ 6 nm spacing. Sub-volume averaging shows the interaction between myosin, tropomyosin and actin in molecular detail at ∼ 10 Å resolution and reveals two coexisting conformations of actin-bound heads. The flexible orientation of the lever arm and the essential and regulatory light chains allow the two heads of the “double-headed” myosin not only to interact with the same actin filament but also to split between two actin filaments. Our results provide new insights into the conformational plasticity and fundamental organisation of vertebrate skeletal muscle and serve as a strong foundation for futurein situinvestigations of muscle diseases.
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影响因子：
3
作者：
Tang, Guang;Peng, Liwei;Ludtke, Steven J.
通讯作者：
Ludtke, Steven J.
影响因子：
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通讯作者：
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影响因子：
16.6
作者：
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影响因子：
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作者：
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