Kensler Robert W
Department of Anatomy, University of Puerto Rico Medical School, Medical Sciences Campus, P.O. Box 365067, San Juan, PR 00936-5067, USA.
J Struct Biol. 2005 Mar;149(3):313-24. doi: 10.1016/j.jsb.2004.12.004.
Information about the structure of the vertebrate striated muscle thick filament backbone is important for understanding the arrangement of both the rod portion of the myosin molecule and the accessory proteins associated with the backbone region of the filament. Although models of the backbone have been proposed, direct data on the structure of the backbone is limited. In this study, we provide evidence that electron micrographs of isolated negatively stained cardiac thick filaments contain significant information about the filament backbone. Computed Fourier transforms from isolated cardiac thick filaments show meridional (or near meridional) reflections on the 10th and 11th layer lines that are particularly strong. Comparison of Fourier filtrations of the filaments that exclude, or include, these reflections, provide evidence that these reflections originate at least in part from a series of striations on the backbone at a approximately 4 nm spacing. The striations are likely to result either from the packing of the myosin rods, or from proteins such as titin associated with the filament backbone.
有关脊椎动物横纹肌粗肌丝主干结构的信息,对于理解肌球蛋白分子的杆状部分以及与肌丝主干区域相关的辅助蛋白的排列至关重要。尽管已经提出了主干的模型,但关于主干结构的直接数据有限。在本研究中,我们提供证据表明,分离的经负染色的心脏粗肌丝的电子显微照片包含有关肌丝主干的重要信息。从分离的心脏粗肌丝计算得到的傅里叶变换显示,在第10层和第11层线上的子午向(或近子午向)反射特别强烈。对排除或包含这些反射的肌丝傅里叶滤波进行比较,提供了证据表明这些反射至少部分源自主干上一系列间距约为4nm的条纹。这些条纹可能是由于肌球蛋白杆的堆积,或者是由于与肌丝主干相关的诸如肌联蛋白等蛋白质所致。