In vitro assembly of the bacterial actin protein MamK from ‘ Candidatus Magnetobacterium casensis’ in the phylum Nitrospirae
ABSTRACT 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 bact...
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| Format: | Article |
| Language: | English |
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Oxford University Press
2016-03-01
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| Series: | Protein & Cell |
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| Online Access: | http://link.springer.com/article/10.1007/s13238-016-0253-x |
| _version_ | 1797715123642564608 |
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| author | Aihua Deng Wei Lin Nana Shi Jie Wu Zhaopeng Sun Qinyun Sun Hua Bai Yongxin Pan Tingyi Wen |
| author_facet | Aihua Deng Wei Lin Nana Shi Jie Wu Zhaopeng Sun Qinyun Sun Hua Bai Yongxin Pan Tingyi Wen |
| author_sort | Aihua Deng |
| collection | DOAJ |
| description | ABSTRACT 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. |
| first_indexed | 2024-03-12T08:02:13Z |
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| institution | Directory Open Access Journal |
| issn | 1674-800X 1674-8018 |
| language | English |
| last_indexed | 2024-03-12T08:02:13Z |
| publishDate | 2016-03-01 |
| publisher | Oxford University Press |
| record_format | Article |
| series | Protein & Cell |
| spelling | doaj.art-ac0f559772ea43b3811c00766e534acc2023-09-02T19:47:54ZengOxford University PressProtein & Cell1674-800X1674-80182016-03-017426728010.1007/s13238-016-0253-xIn vitro assembly of the bacterial actin protein MamK from ‘ Candidatus Magnetobacterium casensis’ in the phylum NitrospiraeAihua Deng0Wei Lin1Nana Shi2Jie Wu3Zhaopeng Sun4Qinyun Sun5Hua Bai6Yongxin Pan7Tingyi Wen8CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of SciencesBiogeomagnetism Group, Paleomagnetism and Geochronology Laboratory, Key Laboratory of Earth and Planetary Physics, Institute of Geology and Geophysics, Chinese Academy of SciencesCAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of SciencesCAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of SciencesCAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of SciencesCAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of SciencesCAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of SciencesBiogeomagnetism Group, Paleomagnetism and Geochronology Laboratory, Key Laboratory of Earth and Planetary Physics, Institute of Geology and Geophysics, Chinese Academy of SciencesCAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of SciencesABSTRACT 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.http://link.springer.com/article/10.1007/s13238-016-0253-xmagnetotactic bacteriaNitrospiraebacterial actinMamKassembly mechanism |
| spellingShingle | Aihua Deng Wei Lin Nana Shi Jie Wu Zhaopeng Sun Qinyun Sun Hua Bai Yongxin Pan Tingyi Wen In vitro assembly of the bacterial actin protein MamK from ‘ Candidatus Magnetobacterium casensis’ in the phylum Nitrospirae Protein & Cell magnetotactic bacteria Nitrospirae bacterial actin MamK assembly mechanism |
| title | In vitro assembly of the bacterial actin protein MamK from ‘ Candidatus Magnetobacterium casensis’ in the phylum Nitrospirae |
| title_full | In vitro assembly of the bacterial actin protein MamK from ‘ Candidatus Magnetobacterium casensis’ in the phylum Nitrospirae |
| title_fullStr | In vitro assembly of the bacterial actin protein MamK from ‘ Candidatus Magnetobacterium casensis’ in the phylum Nitrospirae |
| title_full_unstemmed | In vitro assembly of the bacterial actin protein MamK from ‘ Candidatus Magnetobacterium casensis’ in the phylum Nitrospirae |
| title_short | In vitro assembly of the bacterial actin protein MamK from ‘ Candidatus Magnetobacterium casensis’ in the phylum Nitrospirae |
| title_sort | in vitro assembly of the bacterial actin protein mamk from candidatus magnetobacterium casensis in the phylum nitrospirae |
| topic | magnetotactic bacteria Nitrospirae bacterial actin MamK assembly mechanism |
| url | http://link.springer.com/article/10.1007/s13238-016-0253-x |
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