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In vitroassembly of the bacterial actin protein MamK from ‘CandidatusMagnetobacterium casensis’ in the phylumNitrospirae
Magnetotactic bacteria (MTB), a group of phylogenetically diverse organisms that use their unique intracellular magnetosome organelles to swim along the Earth’s magnetic field, play important roles in the biogeochemical cycles of iron and sulfur. Previous studies have revealed that the bacterial act...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Higher Education Press
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4818849/ https://www.ncbi.nlm.nih.gov/pubmed/26960409 http://dx.doi.org/10.1007/s13238-016-0253-x |
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author | Deng, Aihua Lin, Wei Shi, Nana Wu, Jie Sun, Zhaopeng Sun, Qinyun Bai, Hua Pan, Yongxin Wen, Tingyi |
author_facet | Deng, Aihua Lin, Wei Shi, Nana Wu, Jie Sun, Zhaopeng Sun, Qinyun Bai, Hua Pan, Yongxin Wen, Tingyi |
author_sort | Deng, Aihua |
collection | PubMed |
description | Magnetotactic bacteria (MTB), a group of phylogenetically diverse organisms that use their unique intracellular magnetosome organelles to swim along the Earth’s magnetic field, play important roles in the biogeochemical cycles of iron and sulfur. Previous studies have revealed that the bacterial actin protein MamK plays essential roles in the linear arrangement of magnetosomes in MTB cells belonging to the Proteobacteria phylum. However, the molecular mechanisms of multiple-magnetosome-chain arrangements in MTB remain largely unknown. Here, we report that the MamK filaments from the uncultivated ‘Candidatus Magnetobacterium casensis’ (Mcas) within the phylum Nitrospirae polymerized in the presence of ATP alone and were stable without obvious ATP hydrolysis-mediated disassembly. MamK in Mcas can convert NTP to NDP and NDP to NMP, showing the highest preference to ATP. Unlike its Magnetospirillum counterparts, which form a single magnetosome chain, or other bacterial actins such as MreB and ParM, the polymerized MamK from Mcas is independent of metal ions and nucleotides except for ATP, and is assembled into well-ordered filamentous bundles consisted of multiple filaments. Our results suggest a dynamically stable assembly of MamK from the uncultivated Nitrospirae MTB that synthesizes multiple magnetosome chains per cell. These findings further improve the current knowledge of biomineralization and organelle biogenesis in prokaryotic systems. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1007/s13238-016-0253-x) contains supplementary material, which is available to authorized users. |
format | Online Article Text |
id | pubmed-4818849 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Higher Education Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-48188492016-04-04 In vitroassembly of the bacterial actin protein MamK from ‘CandidatusMagnetobacterium casensis’ in the phylumNitrospirae Deng, Aihua Lin, Wei Shi, Nana Wu, Jie Sun, Zhaopeng Sun, Qinyun Bai, Hua Pan, Yongxin Wen, Tingyi Protein Cell Research Article Magnetotactic bacteria (MTB), a group of phylogenetically diverse organisms that use their unique intracellular magnetosome organelles to swim along the Earth’s magnetic field, play important roles in the biogeochemical cycles of iron and sulfur. Previous studies have revealed that the bacterial actin protein MamK plays essential roles in the linear arrangement of magnetosomes in MTB cells belonging to the Proteobacteria phylum. However, the molecular mechanisms of multiple-magnetosome-chain arrangements in MTB remain largely unknown. Here, we report that the MamK filaments from the uncultivated ‘Candidatus Magnetobacterium casensis’ (Mcas) within the phylum Nitrospirae polymerized in the presence of ATP alone and were stable without obvious ATP hydrolysis-mediated disassembly. MamK in Mcas can convert NTP to NDP and NDP to NMP, showing the highest preference to ATP. Unlike its Magnetospirillum counterparts, which form a single magnetosome chain, or other bacterial actins such as MreB and ParM, the polymerized MamK from Mcas is independent of metal ions and nucleotides except for ATP, and is assembled into well-ordered filamentous bundles consisted of multiple filaments. Our results suggest a dynamically stable assembly of MamK from the uncultivated Nitrospirae MTB that synthesizes multiple magnetosome chains per cell. These findings further improve the current knowledge of biomineralization and organelle biogenesis in prokaryotic systems. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1007/s13238-016-0253-x) contains supplementary material, which is available to authorized users. Higher Education Press 2016-03-09 2016-04 /pmc/articles/PMC4818849/ /pubmed/26960409 http://dx.doi.org/10.1007/s13238-016-0253-x Text en © The Author(s) 2016 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. |
spellingShingle | Research Article Deng, Aihua Lin, Wei Shi, Nana Wu, Jie Sun, Zhaopeng Sun, Qinyun Bai, Hua Pan, Yongxin Wen, Tingyi In vitroassembly of the bacterial actin protein MamK from ‘CandidatusMagnetobacterium casensis’ in the phylumNitrospirae |
title | In vitroassembly of the bacterial actin protein MamK from ‘CandidatusMagnetobacterium casensis’ in the phylumNitrospirae |
title_full | In vitroassembly of the bacterial actin protein MamK from ‘CandidatusMagnetobacterium casensis’ in the phylumNitrospirae |
title_fullStr | In vitroassembly of the bacterial actin protein MamK from ‘CandidatusMagnetobacterium casensis’ in the phylumNitrospirae |
title_full_unstemmed | In vitroassembly of the bacterial actin protein MamK from ‘CandidatusMagnetobacterium casensis’ in the phylumNitrospirae |
title_short | In vitroassembly of the bacterial actin protein MamK from ‘CandidatusMagnetobacterium casensis’ in the phylumNitrospirae |
title_sort | in vitroassembly of the bacterial actin protein mamk from ‘candidatusmagnetobacterium casensis’ in the phylumnitrospirae |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4818849/ https://www.ncbi.nlm.nih.gov/pubmed/26960409 http://dx.doi.org/10.1007/s13238-016-0253-x |
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