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Mol Microbiol. 2010 Apr;76(2):480-8. doi: 10.1111/j.1365-2958.2010.07117.x. Epub 2010 Mar 16.

Identification and functional characterization of liposome tubulation protein from magnetotactic bacteria.

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1
Department of Biotechnology, Tokyo University of Agriculture and Technology, 2-24-16 Naka-cho, Koganei, Tokyo 184-8588, Japan.

Abstract

Magnetotactic bacteria synthesize intracellular magnetosomes that are comprised of membrane-enveloped magnetic crystals. In this study, to identify the early stages of magnetosome formation, we isolated magnetosomes containing small magnetite crystals and those containing regular-sized magnetite crystals from Magnetospirillum magneticum AMB-1. This was achieved by using a novel size fractionation technique, resulting in the identification of a characteristic protein (Amb1018/MamY) from the small magnetite crystal fraction. The gene encoding MamY was located in the magnetosome island. Like the previously reported membrane deformation proteins, such as bin/amphiphysin/Rvs (BAR) and the dynamin family proteins, recombinant MamY protein bound directly to the liposomes, causing them to form long tubules. We established a mamY gene deletion mutant (DeltamamY) and analysed MamY protein localization in it for functional characterization of the protein in vivo. The DeltamamY mutant was found to have expanded magnetosome vesicles and a greater number of small magnetite crystals relative to the wild-type strain, suggesting that the function of the MamY protein is to constrict the magnetosome membrane during magnetosome vesicle formation, following which, the magnetite crystals grow to maturity within them.

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