Tanaka, M., Suwatthanarak, T., Arakaki, A. et al. (5 more authors) (2018) Enhanced tubulation of liposome containing cardiolipin by MamY protein from magnetotactic bacteria. Biotechnology Journal, 13 (12). 1800087. ISSN 1860-6768
Abstract
Lipid tubules are of particular interest for many potential applications in nanotechnology. Among various lipid tubule fabrication techniques, the morphological regulation of membrane structure by proteins mimicking biological processes may provide the chances to form lipid tubes with highly tuned structures. Magnetotactic bacteria synthesize magnetosomes (a unique prokaryotic organelle comprising a magnetite crystal within a lipid envelope). MamY protein is previously identified as the magnetosome protein responsible for magnetosome vesicle formation and stabilization. Furthermore, MamY is shown in vitro liposome tubulation activity. In this study, the interaction of MamY and phospholipids is investigated by using a lipids-immobilized membrane strip and a peptide array. Here, the binding of MamY to the anionic phospholipid, cardiolipin, is found and enhanced liposome tubulation efficiency. The authors propose the interaction is responsible for recruiting and locating cardiolipin to elongate liposome in vitro. The authors also suggest a similar mechanism for the invagination site in magnetosomes vesicle formation, where the lipid itself contributes further to increasing the curvature. These findings are highly important to develop an effective biomimetic synthesis technique of lipid tubules and to elucidate the unique prokaryotic organelle formation in magnetotactic bacteria.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2018 WILEY-VCH Verlag. This is an author produced version of a paper subsequently published in Biotechnology Journal. Uploaded in accordance with the publisher's self-archiving policy. |
Keywords: | cardiolipin; magnetosome; magnetotactic bacteria; membrane tubulation; peptide arrays |
Dates: |
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Institution: | The University of Sheffield |
Academic Units: | The University of Sheffield > Faculty of Science (Sheffield) > Department of Chemistry (Sheffield) |
Depositing User: | Symplectic Sheffield |
Date Deposited: | 23 Nov 2018 14:50 |
Last Modified: | 18 Apr 2024 14:26 |
Status: | Published |
Publisher: | Wiley |
Refereed: | Yes |
Identification Number: | 10.1002/biot.201800087 |
Related URLs: | |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:138573 |