In vitro assembly of the bacterial actin protein MamK from ' Candidatus Magnetobacterium casensis' in the phylum Nitrospirae.
10.1007/s13238-016-0253-x
- Author:
Aihua DENG
1
;
Wei LIN
2
;
Nana SHI
1
;
Jie WU
1
;
Zhaopeng SUN
1
;
Qinyun SUN
1
;
Hua BAI
1
;
Yongxin PAN
2
;
Tingyi WEN
3
Author Information
1. CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing, 100101, China.
2. Biogeomagnetism Group, Paleomagnetism and Geochronology Laboratory, Key Laboratory of Earth and Planetary Physics, Institute of Geology and Geophysics, Chinese Academy of Sciences, Beijing, 100029, China.
3. CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing, 100101, China. wenty@im.ac.cn.
- Publication Type:Journal Article
- Keywords:
MamK;
Nitrospirae;
assembly mechanism;
bacterial actin;
magnetotactic bacteria
- MeSH:
Actins;
chemistry;
metabolism;
Adenosine Triphosphate;
metabolism;
Bacteria;
classification;
metabolism;
Bacterial Proteins;
chemistry;
metabolism;
Magnetospirillum;
classification;
metabolism;
Nucleotides;
metabolism;
Phylogeny;
Substrate Specificity
- From:
Protein & Cell
2016;7(4):267-280
- CountryChina
- Language:English
-
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.
