PuSH - Publication Server of Helmholtz Zentrum München

Gupta, T.K.* ; Klumpe, S.* ; Gries, K.* ; Heinz, S.* ; Wietrzynski, W. ; Ohnishi, N.* ; Niemeyer, J.* ; Spaniol, B.* ; Schaffer, M.* ; Rast, A.* ; Ostermeier, M.* ; Strauss, M.* ; Plitzko, J.M.* ; Baumeister, W.* ; Rudack, T.* ; Sakamoto, W.* ; Nickelsen, J.* ; Schuller, J.M.* ; Schroda, M.* ; Engel, B.D.

Structural basis for VIPP1 oligomerization and maintenance of thylakoid membrane integrity.

Cell 184, 3643-3659.e23 (2021)
DOI Order publishers version
Free by publisher: Publ. Version/Full Text online available 07/2022 Open Access Green: Postprint online available 07/2022
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.
Additional Metrics?
Edit extra informations Login
Publication type Article: Journal article
Document type Scientific Article
Keywords Chlamydomonas ; Clem ; Cryo-electron Tomography ; Cryo-em ; Escrt-iii ; Membrane Remodeling ; Nucleotide Hydrolysis ; Photosynthesis ; Stress Response ; Synechocystis ; Thylakoid Biogenesis; Cryo-em Structure; Shock-protein-a; Vesicle-inducing Protein; Beam-induced Motion; Escrt-iii; Phage-shock; Escherichia-coli; Cryoelectron Tomography; Molecular-dynamics; Bayesian-approach
ISSN (print) / ISBN 0092-8674
e-ISSN 1097-4172
Journal Cell
Quellenangaben Volume: 184, Issue: 14, Pages: 3643-3659.e23 Article Number: , Supplement: ,
Publisher Cell Press
Publishing Place Cambridge, Mass.
Reviewing status Peer reviewed
Institute(s) Helmholtz Pioneer Campus (HPC)
Grants LMU Munich's Institutional Strategy "LMU Excellent''
KAKENHI (Ministry of Education, Culture, Sports, Science and Technology)
KAKENHI (Japanese Society for the Promotion of Science)
Max Planck Society
Helmholtz Zentrum Munchen
Deutsche Forschungsgemeinschaft