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Loss of the actin-like protein MamK has pleiotropic effects on magnetosome formation and chain assembly in Magnetospirillum gryphiswaldense

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Katzmann,  E.
Department of Microbiology, Max Planck Institute for Marine Microbiology, Max Planck Society;

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Scheffel,  A.
Department of Microbiology, Max Planck Institute for Marine Microbiology, Max Planck Society;

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Gruska,  M.
Department of Microbiology, Max Planck Institute for Marine Microbiology, Max Planck Society;

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Plitzko,  J. M.
Department of Microbiology, Max Planck Institute for Marine Microbiology, Max Planck Society;

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Citation

Katzmann, E., Scheffel, A., Gruska, M., Plitzko, J. M., & Schuler, D. (2010). Loss of the actin-like protein MamK has pleiotropic effects on magnetosome formation and chain assembly in Magnetospirillum gryphiswaldense. Molecular Microbiology, 77(1), 208-224.


Cite as: http://hdl.handle.net/21.11116/0000-0001-CB68-6
Abstract
Magnetotactic bacteria synthesize magnetosomes, which are unique organelles consisting of membrane-enclosed magnetite crystals. For magnetic orientation individual magnetosome particles are assembled into well-organized chains. The actin-like MamK and the acidic MamJ proteins were previously implicated in chain assembly. While MamK was suggested to form magnetosome-associated cytoskeletal filaments, MamJ is assumed to attach the magnetosome vesicles to these structures. Although the deletion of either mamK in Magnetospirillum magneticum, or mamJ in Magnetospirillum gryphiswaldense affected chain formation, the previously observed phenotypes were not fully consistent, suggesting different mechanisms of magnetosome chain assembly in both organisms. Here we show that in M. gryphiswaldense MamK is not absolutely required for chain formation. Straight chains, albeit shorter, fragmented and ectopic, were still formed in a mamK deletion mutant, although magnetosome filaments were absent as shown by cryo-electron tomography. Loss of MamK also resulted in reduced numbers of magnetite crystals and magnetosome vesicles and led to the mislocalization of MamJ. In addition, extensive analysis of wild type and mutant cells revealed previously unidentified ultrastructural characteristics in M. gryphiswaldense. Our results suggest that, despite of their functional equivalence, loss of MamK proteins in different bacteria may result in distinct phenotypes, which might be due to a species-specific genetic context.