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Blocking palmitoylation of Toxoplasma gondii myosin light chain 1 disrupts glideosome composition but has little impact on parasite motility

 
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Manage episode 288621572 series 2902311
内容由MultiModal LLC and Multimodal LLC提供。所有播客内容(包括剧集、图形和播客描述)均由 MultiModal LLC and Multimodal LLC 或其播客平台合作伙伴直接上传和提供。如果您认为有人在未经您许可的情况下使用您的受版权保护的作品,您可以按照此处概述的流程进行操作https://zh.player.fm/legal
Link to bioRxiv paper: http://biorxiv.org/cgi/content/short/2020.08.13.250399v1?rss=1 Authors: Rompikuntal, P. K., Foe, I. T., Deng, B., Bogyo, M., WARD, G. E. Abstract: Toxoplasma gondii is a widespread apicomplexan parasite that causes severe disease in immunocompromised individuals and the developing fetus. Like other apicomplexans, T. gondii uses an unusual form of gliding motility to invade cells of its hosts and to disseminate throughout the body during infection. It is well established that a myosin-based motor consisting of a Class XIVa heavy chain (TgMyoA) and two light chains (TgMLC1 and TgELC1/2) plays an important role in parasite motility. The ability of the motor to generate force at the parasite periphery is thought to be reliant upon its anchoring and immobilization within a peripheral membrane-bound compartment, the inner membrane complex (IMC). The motor does not insert into the IMC directly; rather, this interaction is believed to be mediated by the binding of TgMLC1 to the IMC-anchored protein, TgGAP45. The binding of TgMLC1 to TgGAP45 is therefore considered a key element in the force transduction machinery of the parasite. TgMLC1 is palmitoylated, and we show here that palmitoylation occurs on two N-terminal cysteine residues, C8 and C11. Mutations that block TgMLC1 palmitoylation disrupt the association of TgMLC1 with the membrane fraction of the parasite in phase partitioning experiments and completely block the binding of TgMLC1 to TgGAP45. Surprisingly, the loss of TgMLC1 binding to TgGAP45 in these mutant parasites has little effect on their ability to initiate or sustain movement. These results question a key tenet of the current model of apicomplexan motility and suggest that our understanding of gliding motility in this important group of human and animal pathogens is not yet complete. Copy rights belong to original authors. Visit the link for more info
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已归档的系列专辑 ("不活跃的收取点" status)

When? This feed was archived on December 15, 2021 22:10 (2+ y ago). Last successful fetch was on March 29, 2021 12:55 (3y ago)

Why? 不活跃的收取点 status. 我们的伺服器已尝试了一段时间,但仍然无法截取有效的播客收取点

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Manage episode 288621572 series 2902311
内容由MultiModal LLC and Multimodal LLC提供。所有播客内容(包括剧集、图形和播客描述)均由 MultiModal LLC and Multimodal LLC 或其播客平台合作伙伴直接上传和提供。如果您认为有人在未经您许可的情况下使用您的受版权保护的作品,您可以按照此处概述的流程进行操作https://zh.player.fm/legal
Link to bioRxiv paper: http://biorxiv.org/cgi/content/short/2020.08.13.250399v1?rss=1 Authors: Rompikuntal, P. K., Foe, I. T., Deng, B., Bogyo, M., WARD, G. E. Abstract: Toxoplasma gondii is a widespread apicomplexan parasite that causes severe disease in immunocompromised individuals and the developing fetus. Like other apicomplexans, T. gondii uses an unusual form of gliding motility to invade cells of its hosts and to disseminate throughout the body during infection. It is well established that a myosin-based motor consisting of a Class XIVa heavy chain (TgMyoA) and two light chains (TgMLC1 and TgELC1/2) plays an important role in parasite motility. The ability of the motor to generate force at the parasite periphery is thought to be reliant upon its anchoring and immobilization within a peripheral membrane-bound compartment, the inner membrane complex (IMC). The motor does not insert into the IMC directly; rather, this interaction is believed to be mediated by the binding of TgMLC1 to the IMC-anchored protein, TgGAP45. The binding of TgMLC1 to TgGAP45 is therefore considered a key element in the force transduction machinery of the parasite. TgMLC1 is palmitoylated, and we show here that palmitoylation occurs on two N-terminal cysteine residues, C8 and C11. Mutations that block TgMLC1 palmitoylation disrupt the association of TgMLC1 with the membrane fraction of the parasite in phase partitioning experiments and completely block the binding of TgMLC1 to TgGAP45. Surprisingly, the loss of TgMLC1 binding to TgGAP45 in these mutant parasites has little effect on their ability to initiate or sustain movement. These results question a key tenet of the current model of apicomplexan motility and suggest that our understanding of gliding motility in this important group of human and animal pathogens is not yet complete. Copy rights belong to original authors. Visit the link for more info
  continue reading

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