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Giant proteins in a giant cell: Molecular basis of ultrafast Ca(2+)-dependent cell contraction

The giant single-celled eukaryote, Spirostomum, exhibits one of the fastest movements in the biological world. This ultrafast contraction is dependent on Ca(2+) rather than ATP and therefore differs to the actin-myosin system in muscle. We obtained the high-quality genome of Spirostomum minus from w...

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Detalles Bibliográficos
Autores principales: Zhang, Jing, Qin, Weiwei, Hu, Che, Gu, Siyu, Chai, Xiaocui, Yang, Mingkun, Zhou, Fang, Wang, Xueyan, Chen, Kai, Yan, Guanxiong, Wang, Guangying, Jiang, Chuanqi, Warren, Alan, Xiong, Jie, Miao, Wei
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Association for the Advancement of Science 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9946354/
https://www.ncbi.nlm.nih.gov/pubmed/36812318
http://dx.doi.org/10.1126/sciadv.add6550
Descripción
Sumario:The giant single-celled eukaryote, Spirostomum, exhibits one of the fastest movements in the biological world. This ultrafast contraction is dependent on Ca(2+) rather than ATP and therefore differs to the actin-myosin system in muscle. We obtained the high-quality genome of Spirostomum minus from which we identified the key molecular components of its contractile apparatus, including two major Ca(2+) binding proteins (Spasmin 1 and 2) and two giant proteins (GSBP1 and GSBP2), which act as the backbone and allow for the binding of hundreds of spasmins. The evidence suggests that the GSBP-spasmin protein complex is the functional unit of the mesh-like contractile fibrillar system, which, coupled with various other subcellular structures, provides the mechanism for repetitive ultrafast cell contraction and extension. These findings improve our understanding of the Ca(2+)-dependent ultrafast movement and provide a blueprint for future biomimicry, design, and construction of this kind of micromachine.