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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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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
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author 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
author_facet 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
author_sort Zhang, Jing
collection PubMed
description 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.
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spelling pubmed-99463542023-02-23 Giant proteins in a giant cell: Molecular basis of ultrafast Ca(2+)-dependent cell contraction 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 Sci Adv Biomedicine and Life Sciences 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. American Association for the Advancement of Science 2023-02-22 /pmc/articles/PMC9946354/ /pubmed/36812318 http://dx.doi.org/10.1126/sciadv.add6550 Text en Copyright © 2023 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works. Distributed under a Creative Commons Attribution NonCommercial License 4.0 (CC BY-NC). https://creativecommons.org/licenses/by-nc/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution-NonCommercial license (https://creativecommons.org/licenses/by-nc/4.0/) , which permits use, distribution, and reproduction in any medium, so long as the resultant use is not for commercial advantage and provided the original work is properly cited.
spellingShingle Biomedicine and Life Sciences
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
Giant proteins in a giant cell: Molecular basis of ultrafast Ca(2+)-dependent cell contraction
title Giant proteins in a giant cell: Molecular basis of ultrafast Ca(2+)-dependent cell contraction
title_full Giant proteins in a giant cell: Molecular basis of ultrafast Ca(2+)-dependent cell contraction
title_fullStr Giant proteins in a giant cell: Molecular basis of ultrafast Ca(2+)-dependent cell contraction
title_full_unstemmed Giant proteins in a giant cell: Molecular basis of ultrafast Ca(2+)-dependent cell contraction
title_short Giant proteins in a giant cell: Molecular basis of ultrafast Ca(2+)-dependent cell contraction
title_sort giant proteins in a giant cell: molecular basis of ultrafast ca(2+)-dependent cell contraction
topic Biomedicine and Life Sciences
url 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
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