A highly active bacterial actin actuates the polymerization of another isoform essential for swimming motility of Spiroplasma

Daichi Takahashi, Hana Kiyama, Hideaki Matsubayashi, Ikuko Fujiwara, Makoto Miyata
{"title":"A highly active bacterial actin actuates the polymerization of another isoform essential for swimming motility of Spiroplasma","authors":"Daichi Takahashi, Hana Kiyama, Hideaki Matsubayashi, Ikuko Fujiwara, Makoto Miyata","doi":"10.1101/2024.09.04.611326","DOIUrl":null,"url":null,"abstract":"<em>Spiroplasma</em> is a wall−less helical bacterium possessing five isoforms of bacterial actin MreBs (SMreB1−5) for its swimming, speculated to be the sole motility system driven by endogenous bacterial actin proteins. Its detailed molecular mechanism remains elusive due to the lack of soluble constructs of SMreB1 essential for <em>Spiroplasma</em> swimming. Here, we isolated soluble SMreB1 of <em>Spiroplasma eriocheiris </em>(SpeMreB1) and evaluated its activity. The phosphate release rate and fold changes of polymerization−critical concentrations over the nucleotide states of SpeMreB1 are the highest among the MreB family proteins. SpeMreB1 interacts with polymerized SpeMreB5, another SMreB essential for <em>Spiroplasma</em> swimming, and decreases SpeMreB5 filament amount depending on the nucleotide state. A decrease in SpeMreB5 filament amount is independent of SpeMreB1 polymerization, although it is essential for swimming motility. SpeMreB1 binds to negatively charged lipids, regardless of their nucleotide state. These results suggest that SpeMreB1 manages SpeMreB5 filaments to drive <em>Spiroplasma</em> swimming.","PeriodicalId":501048,"journal":{"name":"bioRxiv - Biophysics","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"2024-09-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"bioRxiv - Biophysics","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1101/2024.09.04.611326","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 0

Abstract

Spiroplasma is a wall−less helical bacterium possessing five isoforms of bacterial actin MreBs (SMreB1−5) for its swimming, speculated to be the sole motility system driven by endogenous bacterial actin proteins. Its detailed molecular mechanism remains elusive due to the lack of soluble constructs of SMreB1 essential for Spiroplasma swimming. Here, we isolated soluble SMreB1 of Spiroplasma eriocheiris (SpeMreB1) and evaluated its activity. The phosphate release rate and fold changes of polymerization−critical concentrations over the nucleotide states of SpeMreB1 are the highest among the MreB family proteins. SpeMreB1 interacts with polymerized SpeMreB5, another SMreB essential for Spiroplasma swimming, and decreases SpeMreB5 filament amount depending on the nucleotide state. A decrease in SpeMreB5 filament amount is independent of SpeMreB1 polymerization, although it is essential for swimming motility. SpeMreB1 binds to negatively charged lipids, regardless of their nucleotide state. These results suggest that SpeMreB1 manages SpeMreB5 filaments to drive Spiroplasma swimming.
一种高活性细菌肌动蛋白促使螺浆虫游泳运动所必需的另一种同工酶聚合
螺浆菌是一种无壁螺旋细菌,拥有五种细菌肌动蛋白 MreBs(SMreB1-5)异构体,用于游动,据推测这是唯一由内源性细菌肌动蛋白驱动的运动系统。由于缺乏螺浆游动所必需的 SMreB1 的可溶性构建体,其详细的分子机制仍然难以确定。在此,我们分离了螺旋体eriocheiris的可溶性SMreB1(SpeMreB1)并评估了其活性。在 MreB 家族蛋白中,SpeMreB1 的磷酸释放率和聚合临界浓度随核苷酸状态变化的倍数是最高的。SpeMreB1 与聚合的 SpeMreB5(螺浆游动所必需的另一种 SMreB)相互作用,并根据核苷酸状态减少 SpeMreB5 的丝量。SpeMreB5 细丝数量的减少与 SpeMreB1 的聚合无关,尽管它对游动至关重要。无论核苷酸状态如何,SpeMreB1 都能与带负电荷的脂质结合。这些结果表明,SpeMreB1管理着SpeMreB5丝,从而驱动螺浆虫游动。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 求助全文
来源期刊
自引率
0.00%
发文量
0
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术官方微信