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  Structural basis for VIPP1 oligomerization and maintenance of thylakoid membrane integrity

Gupta, T. K., Klumpe, S., Gries, K., Heinz, S., Wietrzynski, W., Ohnishi, N., et al. (2021). Structural basis for VIPP1 oligomerization and maintenance of thylakoid membrane integrity. Cell, 184(14), 3643-3659.e23. doi:10.1016/j.cell.2021.05.011.

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 Creators:
Gupta, Tilak Kumar1, Author              
Klumpe, Sven1, Author              
Gries, Karin2, Author
Heinz, Steffen2, Author
Wietrzynski, Wojciech1, Author              
Ohnishi, Norikazu2, Author
Niemeyer, Justus2, Author
Spaniol, Benjamin2, Author
Schaffer, Miroslava1, Author              
Rast, Anna1, Author              
Ostermeier, Matthias2, Author
Strauss, Mike2, Author
Plitzko, Jürgen M.1, Author              
Baumeister, Wolfgang1, Author              
Rudack, Till2, Author
Sakamoto, Wataru2, Author
Nickelsen, Joerg2, Author
Schuller, Jan M.2, Author
Schroda, Michael2, Author
Engel, Benjamin D.1, Author              
Affiliations:
1Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565142              
2external, ou_persistent22              

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Free keywords: CRYO-EM STRUCTURE; SHOCK-PROTEIN-A; VESICLE-INDUCING PROTEIN; BEAM-INDUCED MOTION; ESCRT-III; PHAGE-SHOCK; ESCHERICHIA-COLI; CRYOELECTRON TOMOGRAPHY; MOLECULAR-DYNAMICS; BAYESIAN-APPROACHBiochemistry & Molecular Biology; Cell Biology;
 Abstract: Vesicle-inducing protein in plastids 1 (VIPP1) is essential for the biogenesis and maintenance of thylakoid membranes, which transform light into life. However, it is unknown how VIPP1 performs its vital membrane-remodeling functions. Here, we use cryo-electron microscopy to determine structures of cyanobacterial VIPP1 rings, revealing how VIPP1 monomers flex and interweave to form basket-like assemblies of different symmetries. Three VIPP1 monomers together coordinate a non-canonical nucleotide binding pocket on one end of the ring. Inside the ring's lumen, amphipathic helices from each monomer align to form large hydrophobic columns, enabling VIPP1 to bind and curve membranes. In vivo mutations in these hydrophobic surfaces cause extreme thylakoid swelling under high light, indicating an essential role of VIPP1 lipid binding in resisting stress-induced damage. Using cryo-correlative light and electron microscopy (cryo-CLEM), we observe oligomeric VIPP1 coats encapsulating membrane tubules within the Chlamydomonas chloroplast. Our work provides a structural foundation for understanding how VIPP1 directs thylakoid biogenesis and maintenance.

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Language(s): eng - English
 Dates: 2021
 Publication Status: Published in print
 Pages: 40
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Degree: -

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Title: Cell
Source Genre: Journal
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Publ. Info: Cambridge, Mass. : Cell Press
Pages: - Volume / Issue: 184 (14) Sequence Number: - Start / End Page: 3643 - 3659.e23 Identifier: ISSN: 0092-8674
CoNE: https://pure.mpg.de/cone/journals/resource/954925463183