Magnetotactic bacteria （MTB）, a group of phylogeneti- cally diverse organisms that use their unique intracellular magnetosome organelles to swim along the Earth＇s magnetic field, play important roles in the biogeoc...Magnetotactic bacteria （MTB）, a group of phylogeneti- cally 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 multi- ple-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.展开更多
基金ACKNOWLEDGEMENTS The authors would like to thank Rongcheng Han, Yabing Liu and Xiaolan Zhang for assistance with the fluorescence microscopy, and Jingnan Liang for assistance with transmission electron microscopy. This work was supported by the grants from the National Natural Science Foundation of China （Grants Nos. 31300065 and 41330104） and the Youth Innovation Promotion Association CAS.
文摘Magnetotactic bacteria （MTB）, a group of phylogeneti- cally 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 multi- ple-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.
