Protruding masticatory (superfast) myosin heads from poorly aligned thick filaments of dog jaw muscle revealed by X-ray diffraction
Protruding masticatory (superfast) myosin heads from poorly aligned thick filaments of dog jaw muscle revealed by X-ray diffraction
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X 射线衍射显示,狗下巴肌肉排列不良的粗细丝中突出的咀嚼(超快)肌球蛋白头
DOI:
10.1093/jb/mvp143
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发表时间:
2010
期刊:
影响因子:
--
通讯作者:
Y.
中科院分区:
文献类型:
--
作者:
Yamaguchi;M.;Takemori;S.;Kimura;M.;Tanishima;Y.;Nakayoshi;T.;Kimura;S.;Ohno;T.;Yagi;N.;Hoh;F.Y. J.;Umazume;Y.
To characterize the structure of jaw muscle fibres expressing masticatory (superfast) myosin, X-ray diffraction patterns of glycerinated fibres of dogmasseterwere compared with those of dogtibialis anteriorin the relaxed state. Meridional reflections ofmasseterfibres were laterally broad, indicating that myosin filaments are staggered along the filament axis. Compared withtibialis anteriorfibres, the peak of the first myosin layer line ofmasseterfibres was lower in intensity and shifted towards the meridian, while lattice spacings were larger at a similar sarcomere length. These suggest that the myosin heads of masticatory fibres are mobile, and tend to protrude from the filament shaft towards actin filaments. Lowering temperature or treating withN-phenylmaleimide shifted the peak of the first myosin layer line oftibialis anteriorfibres towards the meridian and the resulting profile resembled that ofmasseterfibres. This suggests that the protruding mobile heads in the non-treated masticatory fibres are in the ATP-bound state. The increased population of weakly binding cross-bridges may contribute towards the high specific force of masticatory fibres during contraction. Electron micrographs confirmed the staggered alignment of thick filaments along the filament axis within sarcomeres of masticatory fibres, a feature that may confer efficient force development over a wide range of the sarcomere lengths.