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The dual role of MamB in magnetosome membrane assembly and magnetite biomineralization

URN to cite this document: urn:nbn:de:bvb:703-epub-4319-8

Title data

Uebe, René ; Keren-Khadmy, Noa ; Zeytuni, Natalie ; Katzmann, Emanuel ; Navon, Yotam ; Davidov, Geula ; Bitton, Ronit ; Plitzko, Jürgen M. ; Schüler, Dirk ; Zarivach, Raz:
The dual role of MamB in magnetosome membrane assembly and magnetite biomineralization.
Bayreuth, Germany , 2017

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Project information

Project title:
Project's official titleProject's id
European Union’s Horizon 2020 research and innovation programme692637

Project financing: European Research Council (ERC)
Israel Ministry of Science, Technology and Space (R.Z.)
Israel Science Foundation (grant No. 167/16; R.Z.)
European Molecular Biology Organization and CMST COST Action CM1306 (R.Z.)

Abstract

Magnetospirillum gryphiswaldense MSR-1 synthesizes membrane-enclosed magnetite (Fe3O4) nanoparticles, magnetosomes, for magnetotaxis. Formation of these organelles involves a complex process comprising key steps which are governed by specific magnetosome-associated proteins. MamB, a cation diffusion facilitator (CDF) family member has been implicated in magnetosome-directed iron transport. However, deletion mutagenesis studies revealed that MamB is essential for the formation of magnetosome membrane vesicles, but its precise role remains elusive. In this study, we employed a multi-disciplinary approach to define the role of MamB during magnetosome formation. Using site-directed mutagenesis complemented by structural analyses, fluorescence microscopy and cryo-electron tomography, we show that MamB is most likely an active magnetosome-directed transporter serving two distinct, yet essential functions. First, MamB initiates magnetosome vesicle formation in a transport-independent process, probably by serving as a landmark protein. Second, MamB transport activity is required for magnetite nucleation. Furthermore, by determining the crystal structure of the MamB cytosolic C-terminal domain, we also provide mechanistic insight into transport regulation. Additionally, we present evidence that magnetosome vesicle growth and chain formation are independent of magnetite nucleation and magnetic interactions, respectively. Together, our data provide novel insight into the role of the key bifunctional magnetosome protein MamB, and the early steps of magnetosome formation.

Further data

Item Type: Preprint, postprint
Additional notes (visible to public): In: Molecular Microbiology, Bd. 107 (2018)Heft 4, S. 542-557
This project has received funding from the European Research Council (ERC) under the European Union’s Horizon 2020 research and innovation programme (grant agreement No 692637, D.S.) and the Israel Ministry of Science, Technology and Space (R.Z.), the Israel Science Foundation (grant No. 167/16; R.Z.), the European Molecular Biology Organization and CMST COST Action CM1306 (R.Z.).
Keywords: Bacterial organelle; biomineralization; cation diffusion facilitators; iron transport; magnetosome biogenesis; magnetotactic bacteria; membrane invagination; structure-function analysis
DDC Subjects: 500 Science > 570 Life sciences, biology
Institutions of the University: Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Biology > Chair Microbiology > Chair Microbiology - Univ.-Prof. Dr. Dirk Schüler
Faculties
Faculties > Faculty of Biology, Chemistry and Earth Sciences
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Biology
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Biology > Chair Microbiology
Language: English
Originates at UBT: Yes
URN: urn:nbn:de:bvb:703-epub-4319-8
Date Deposited: 25 Apr 2019 10:57
Last Modified: 25 Apr 2019 10:57
URI: https://epub.uni-bayreuth.de/id/eprint/4319

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