The actomyosin interface contains an evolutionary conserved core and an ancillary interface involved in specificity.
The actomyosin interface contains an evolutionary conserved core and an ancillary interface involved in specificity.
复制标题
DOI：
10.1038/s41467-021-22093-4
复制
发表时间：
2021-03-25
影响因子：
16.6
通讯作者：
Hanein D
中科院分区：
文献类型：
--
作者：
Robert-Paganin J;Xu XP;Swift MF;Auguin D;Robblee JP;Lu H;Fagnant PM;Krementsova EB;Trybus KM;Houdusse A;Volkmann N;Hanein D
恶性疟原虫，疟疾的病原体，通过一种被称为滑动运动的非典型过程移动。肌动球蛋白的相互作用是滑翔运动的核心。然而，直到现在，这些相互作用的细节仍然难以捉摸。在这里，我们报告了在动力冲程结束时用电子冷冻显微镜测定的恶性疟原虫肌动球蛋白系统的原子结构。该结构提供了对寄生虫产生感染性所需的力和运动所需的详细相互作用的见解。值得注意的是，肌凝蛋白马达在丝状肌动蛋白上的足迹相对于高等真核生物是保守的，尽管恶性疟原虫肌凝蛋白和肌动蛋白元件构成界面的重要变异性。与其他肌动球蛋白复合物比较，发现所有肌动球蛋白复合物都有一个保守的核心界面，并有一个辅助界面参与定义肌动蛋白丝上马达的空间定位。恶性疟原虫通过一种称为滑动运动的非典型过程移动，该过程由非典型肌球蛋白A （PfMyoA）和动态和分化的PfActin-1 （PfAct1）的细丝组成。在这里，作者展示了PfMyoA与丝状PfAct1结合的低温电镜结构，并提供了寄生虫产生感染性所需的力和运动所需的相互作用的见解。
Plasmodium falciparum, the causative agent of malaria, moves by an atypical process called gliding motility. Actomyosin interactions are central to gliding motility. However, the details of these interactions remained elusive until now. Here, we report an atomic structure of the divergent Plasmodium falciparum actomyosin system determined by electron cryomicroscopy at the end of the powerstroke (Rigor state). The structure provides insights into the detailed interactions that are required for the parasite to produce the force and motion required for infectivity. Remarkably, the footprint of the myosin motor on filamentous actin is conserved with respect to higher eukaryotes, despite important variability in the Plasmodium falciparum myosin and actin elements that make up the interface. Comparison with other actomyosin complexes reveals a conserved core interface common to all actomyosin complexes, with an ancillary interface involved in defining the spatial positioning of the motor on actin filaments. Plasmodium falciparum moves by an atypical process called gliding motility which comprises of atypical myosin A (PfMyoA) and filaments of the dynamic and divergent PfActin-1 (PfAct1). Here authors present the cryo-EM structure of PfMyoA bound to filamentous PfAct1 stabilized with jasplakinolide and provide insights into the interactions that are required for the parasite to produce the force and motion required for infectivity.
登录
查看更多内容
影响因子：
9.8
作者：
Kumpula, Esa-Pekka;Lopez, Andrea J.;Kursula, Inari
通讯作者：
Kursula, Inari
影响因子：
48
作者：
Barad BA;Echols N;Wang RY;Cheng Y;DiMaio F;Adams PD;Fraser JS
通讯作者：
Fraser JS
影响因子：
48
作者：
Kucukelbir, Alp;Sigworth, Fred J.;Tagare, Hemant D.
通讯作者：
Tagare, Hemant D.
影响因子：
3
作者：
Banerjee, Chaity;Hu, Zhongjun;Taylor, Kenneth A.
通讯作者：
Taylor, Kenneth A.
DOI：
10.3109/10409238.2013.821444
发表时间：
2013-07
影响因子：
6.5
作者：
Koumandou VL;Wickstead B;Ginger ML;van der Giezen M;Dacks JB;Field MC
通讯作者：
Field MC