Structure of the Flight Muscle Thick Filament from the Bumble Bee, Bombus ignitus, at 6 Å Resolution.

Structure of the Flight Muscle Thick Filament from the Bumble Bee, Bombus ignitus, at 6 Å Resolution.
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DOI:
10.3390/ijms24010377
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发表时间:
2022-12-26
影响因子:
5.6
通讯作者:
Taylor, Kenneth A.
Taylor, Kenneth A.
中科院分区:
生物学2区
文献类型:
--
作者:
Li, Jiawei;Rahmani, Hamidreza;Yeganeh, Fatemeh Abbasi;Rastegarpouyani, Hosna;Taylor, Dianne W.;Wood, Neil B.;Previs, Michael J.;Iwamoto, Hiroyuki;Taylor, Kenneth A.

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四种昆虫目具有异步和间接的飞行肌肉;它们是异步的,因为翅膀的拍动频率与神经刺激的频率脱钩;它们是间接的,因为肌肉附着在胸部外骨骼上,而不是直接附着在翅膀上。来自半翅目和双翅目两个目的飞行肌粗丝已以亚纳米分辨率成像,这两种图像都揭示了被称为“弯曲分子结晶层”的肌球蛋白尾部排列。在这里,我们报告了来自第三种昆虫膜翅目、亚洲大黄蜂 Bombus ignitus 的间接飞行肌肉的粗丝结构。肌球蛋白尾部与之前对 Lethocerus indicus 和 Drosophila melanogaster 的测定结果基本一致。 Skip 2 区域具有与 Lethocerus indicus 粗丝相同的不寻常结构,Skip 4 处也可见 α 螺旋不连续性,但与其他两个物种相比,Skip 1 区域在主干表面上的方向相对于丝轴的角度较小。头部与果蝇一样是无序的,但我们在主干表面上没有观察到非肌球蛋白蛋白质,这可能会阻止肌球蛋白头部在粗丝主干上的排序。这三个物种的主干内的非肌球蛋白具有很强的结构相似性,这表明如何对 Lethocerus 中一种先前未分配的密度进行分配。总体而言,该结构符合先前观察到的肌球蛋白尾部排列高度相似的模式,但非肌球蛋白蛋白质存在差异。
Four insect orders have flight muscles that are both asynchronous and indirect; they are asynchronous in that the wingbeat frequency is decoupled from the frequency of nervous stimulation and indirect in that the muscles attach to the thoracic exoskeleton instead of directly to the wing. Flight muscle thick filaments from two orders, Hemiptera and Diptera, have been imaged at a subnanometer resolution, both of which revealed a myosin tail arrangement referred to as “curved molecular crystalline layers”. Here, we report a thick filament structure from the indirect flight muscles of a third insect order, Hymenoptera, the Asian bumble bee Bombus ignitus. The myosin tails are in general agreement with previous determinations from Lethocerus indicus and Drosophila melanogaster. The Skip 2 region has the same unusual structure as found in Lethocerus indicus thick filaments, an α-helix discontinuity is also seen at Skip 4, but the orientation of the Skip 1 region on the surface of the backbone is less angled with respect to the filament axis than in the other two species. The heads are disordered as in Drosophila, but we observe no non-myosin proteins on the backbone surface that might prohibit the ordering of myosin heads onto the thick filament backbone. There are strong structural similarities among the three species in their non-myosin proteins within the backbone that suggest how one previously unassigned density in Lethocerus might be assigned. Overall, the structure conforms to the previously observed pattern of high similarity in the myosin tail arrangement, but differences in the non-myosin proteins.
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