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MamY is a membrane-bound protein that aligns magnetosomes and the motility axis of helical magnetotactic bacteria

To navigate within the geomagnetic field, magnetotactic bacteria synthesize magnetosomes, which are unique organelles consisting of membrane-enveloped magnetite nanocrystals. In magnetotactic spirilla, magnetosomes become actively organized into chains by the filament-forming actin-like MamK and the...

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Autores principales: Toro-Nahuelpan, Mauricio, Giacomelli, Giacomo, Raschdorf, Oliver, Borg, Sarah, Plitzko, Jürgen M., Bramkamp, Marc, Schüler, Dirk, Müller, Frank-Dietrich
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6817358/
https://www.ncbi.nlm.nih.gov/pubmed/31358981
http://dx.doi.org/10.1038/s41564-019-0512-8
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author Toro-Nahuelpan, Mauricio
Giacomelli, Giacomo
Raschdorf, Oliver
Borg, Sarah
Plitzko, Jürgen M.
Bramkamp, Marc
Schüler, Dirk
Müller, Frank-Dietrich
author_facet Toro-Nahuelpan, Mauricio
Giacomelli, Giacomo
Raschdorf, Oliver
Borg, Sarah
Plitzko, Jürgen M.
Bramkamp, Marc
Schüler, Dirk
Müller, Frank-Dietrich
author_sort Toro-Nahuelpan, Mauricio
collection PubMed
description To navigate within the geomagnetic field, magnetotactic bacteria synthesize magnetosomes, which are unique organelles consisting of membrane-enveloped magnetite nanocrystals. In magnetotactic spirilla, magnetosomes become actively organized into chains by the filament-forming actin-like MamK and the adaptor protein MamJ, thereby assembling a magnetic dipole much like a compass needle. However, in Magnetospirillum gryphiswaldense, discontinuous chains are still formed in the absence of MamK. Moreover, these fragmented chains persist in a straight conformation indicating undiscovered structural determinants able to accommodate a bar magnet-like magnetoreceptor in a helical bacterium. Here, we identify MamY, a membrane-bound protein that generates a sophisticated mechanical scaffold for magnetosomes. MamY localizes linearly along the positive inner cell curvature (the geodetic cell axis) likely by self-interaction and curvature sensing. In a mamY deletion mutant, magnetosome chains detach from the geodetic axis and fail to accommodate a straight conformation coinciding with reduced cellular magnetic orientation. Co-deletion of mamKY completely abolishes chain formation, whereas upon synthetic tethering of magnetosomes to MamY, the chain configuration is regained, emphasizing the structural properties of the protein. Our results suggest MamY as membrane-anchored mechanical scaffold essential to align the motility axis of magnetotactic spirilla with their magnetic moment vector and to perfectly reconcile magnetoreception with swimming direction.
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spelling pubmed-68173582020-01-29 MamY is a membrane-bound protein that aligns magnetosomes and the motility axis of helical magnetotactic bacteria Toro-Nahuelpan, Mauricio Giacomelli, Giacomo Raschdorf, Oliver Borg, Sarah Plitzko, Jürgen M. Bramkamp, Marc Schüler, Dirk Müller, Frank-Dietrich Nat Microbiol Article To navigate within the geomagnetic field, magnetotactic bacteria synthesize magnetosomes, which are unique organelles consisting of membrane-enveloped magnetite nanocrystals. In magnetotactic spirilla, magnetosomes become actively organized into chains by the filament-forming actin-like MamK and the adaptor protein MamJ, thereby assembling a magnetic dipole much like a compass needle. However, in Magnetospirillum gryphiswaldense, discontinuous chains are still formed in the absence of MamK. Moreover, these fragmented chains persist in a straight conformation indicating undiscovered structural determinants able to accommodate a bar magnet-like magnetoreceptor in a helical bacterium. Here, we identify MamY, a membrane-bound protein that generates a sophisticated mechanical scaffold for magnetosomes. MamY localizes linearly along the positive inner cell curvature (the geodetic cell axis) likely by self-interaction and curvature sensing. In a mamY deletion mutant, magnetosome chains detach from the geodetic axis and fail to accommodate a straight conformation coinciding with reduced cellular magnetic orientation. Co-deletion of mamKY completely abolishes chain formation, whereas upon synthetic tethering of magnetosomes to MamY, the chain configuration is regained, emphasizing the structural properties of the protein. Our results suggest MamY as membrane-anchored mechanical scaffold essential to align the motility axis of magnetotactic spirilla with their magnetic moment vector and to perfectly reconcile magnetoreception with swimming direction. 2019-07-29 2019-11 /pmc/articles/PMC6817358/ /pubmed/31358981 http://dx.doi.org/10.1038/s41564-019-0512-8 Text en http://www.nature.com/authors/editorial_policies/license.html#terms Users may view, print, copy, and download text and data-mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use:http://www.nature.com/authors/editorial_policies/license.html#terms
spellingShingle Article
Toro-Nahuelpan, Mauricio
Giacomelli, Giacomo
Raschdorf, Oliver
Borg, Sarah
Plitzko, Jürgen M.
Bramkamp, Marc
Schüler, Dirk
Müller, Frank-Dietrich
MamY is a membrane-bound protein that aligns magnetosomes and the motility axis of helical magnetotactic bacteria
title MamY is a membrane-bound protein that aligns magnetosomes and the motility axis of helical magnetotactic bacteria
title_full MamY is a membrane-bound protein that aligns magnetosomes and the motility axis of helical magnetotactic bacteria
title_fullStr MamY is a membrane-bound protein that aligns magnetosomes and the motility axis of helical magnetotactic bacteria
title_full_unstemmed MamY is a membrane-bound protein that aligns magnetosomes and the motility axis of helical magnetotactic bacteria
title_short MamY is a membrane-bound protein that aligns magnetosomes and the motility axis of helical magnetotactic bacteria
title_sort mamy is a membrane-bound protein that aligns magnetosomes and the motility axis of helical magnetotactic bacteria
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6817358/
https://www.ncbi.nlm.nih.gov/pubmed/31358981
http://dx.doi.org/10.1038/s41564-019-0512-8
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