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Magnetite biomineralization in Magnetospirillum magneticum is regulated by a switch-like behavior in the HtrA protease MamE

David M. Hershey, Patrick J. Browne, Anthony T. Iavarone, Joan Teyra, Eun H. Lee, Sachdev S. Sidhu, Arash Komeili
doi: https://doi.org/10.1101/047555
David M. Hershey
1Department of Plant and Microbial Biology, University of California, Berkeley, CA 94720, USA
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Patrick J. Browne
1Department of Plant and Microbial Biology, University of California, Berkeley, CA 94720, USA
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Anthony T. Iavarone
2California Institute for Quantitative Biosciences, University of California, Berkeley, CA 94720, USA
3QB3/Chemistry Mass Spectrometry Facility, University of California, Berkeley, CA 94720, USA
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Joan Teyra
4Department of Molecular Genetics, Terrance Donnelly Centre for Cellular and Biomedical Research, University of Toronto, Toronto, Canada ON M5S 3E1
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Eun H. Lee
5Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720, USA
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Sachdev S. Sidhu
4Department of Molecular Genetics, Terrance Donnelly Centre for Cellular and Biomedical Research, University of Toronto, Toronto, Canada ON M5S 3E1
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Arash Komeili
1Department of Plant and Microbial Biology, University of California, Berkeley, CA 94720, USA
2California Institute for Quantitative Biosciences, University of California, Berkeley, CA 94720, USA
5Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720, USA
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  • For correspondence: komeili@berkeley.edu
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Abstract

Magnetotactic bacteria are aquatic organisms that produce subcellular magnetic particles in order to orient in the earth’s geomagnetic field. MamE, a predicted HtrA protease required to produce magnetite crystals in the magnetotactic bacterium Magnetospirillum magneticum AMB-1, was recently shown to promote the proteolytic processing of itself and two other biomineralization factors in vivo. Here, we have analyzed the in vivo processing patterns of three proteolytic targets and used this information to reconstitute proteolysis with a purified form of MamE in vitro. MamE cleaves a custom peptide substrate with positive cooperativity, and its auto-proteolysis can be stimulated with exogenous substrates or peptides that bind to either of its PDZ domains. A misregulated form of the protease that circumvents specific genetic requirements for proteolysis causes biomineralization defects, showing that proper regulation of its activity is required during magnetite biosynthesis in vivo. Our results represent the first reconstitution of MamE’s proteolytic activity and show that its behavior is consistent with the previously proposed checkpoint model for biomineralization.

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Posted June 07, 2016.
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Magnetite biomineralization in Magnetospirillum magneticum is regulated by a switch-like behavior in the HtrA protease MamE
David M. Hershey, Patrick J. Browne, Anthony T. Iavarone, Joan Teyra, Eun H. Lee, Sachdev S. Sidhu, Arash Komeili
bioRxiv 047555; doi: https://doi.org/10.1101/047555
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Magnetite biomineralization in Magnetospirillum magneticum is regulated by a switch-like behavior in the HtrA protease MamE
David M. Hershey, Patrick J. Browne, Anthony T. Iavarone, Joan Teyra, Eun H. Lee, Sachdev S. Sidhu, Arash Komeili
bioRxiv 047555; doi: https://doi.org/10.1101/047555

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