Department of Microbiology and Molecular Medicine, CMU, University of Geneva, 1 Rue Michel-Servet, CH-1211 Geneva 4, Switzerland.
Traffic. 2011 Mar;12(3):287-300. doi: 10.1111/j.1600-0854.2010.01148.x. Epub 2011 Jan 7.
Toxoplasma gondii possesses 11 rather atypical myosin heavy chains. The only myosin light chain described to date is MLC1, associated with myosin A, and contributing to gliding motility. In this study, we examined the repertoire of calmodulin-like proteins in Apicomplexans, identified six putative myosin light chains and determined their subcellular localization in T. gondii and Plasmodium falciparum. MLC2, only found in coccidians, is associated with myosin D via its calmodulin (CaM)-like domain and anchored to the plasma membrane of T. gondii via its N-terminal extension. Molecular modeling suggests that the MyoD-MLC2 complex is more compact than the reported structure of Plasmodium MyoA-myosin A tail-interacting protein (MTIP) complex. Anchorage of this MLC2 to the plasma membrane is likely governed by palmitoylation.
刚地弓形虫拥有 11 种相当非典型的肌球蛋白重链。迄今为止，描述的唯一肌球蛋白轻链是 MLC1，与肌球蛋白 A 相关，并有助于滑行运动。在这项研究中，我们研究了顶复门生物中的钙调蛋白样蛋白谱，鉴定了六个假定的肌球蛋白轻链，并确定了它们在刚地弓形虫和恶性疟原虫中的亚细胞定位。仅在球虫中发现的 MLC2 通过其钙调蛋白（CaM）样结构域与肌球蛋白 D 相关，并通过其 N 端延伸锚定在刚地弓形虫的质膜上。分子建模表明，MyoD-MLC2 复合物比报道的恶性疟原虫 MyoA-肌球蛋白 A 尾相互作用蛋白（MTIP）复合物的结构更紧凑。这种 MLC2 与质膜的锚定可能受棕榈酰化控制。
