Details

Autor(en) / Beteiligte

• Gupta, Tilak Kumar
• Klumpe, Sven
• Gries, Karin
• Heinz, Steffen
• Wietrzynski, Wojciech
• Ohnishi, Norikazu
• Niemeyer, Justus
• Spaniol, Benjamin
• Schaffer, Miroslava
• Rast, Anna
• Ostermeier, Matthias
• Strauss, Mike
• Plitzko, Jürgen M.
• Baumeister, Wolfgang
• Rudack, Till
• Sakamoto, Wataru
• Nickelsen, Jörg
• Schuller, Jan M.
• Schroda, Michael
• Engel, Benjamin D.

Titel

Structural basis for VIPP1 oligomerization and maintenance of thylakoid membrane integrity

Ist Teil von

• Cell, 2021-07, Vol.184 (14), p.3643-3659.e23

Ort / Verlag

United States: Elsevier Inc

Erscheinungsjahr

2021

Quelle

MEDLINE

Beschreibungen/Notizen

• 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. [Display omitted] •Cryo-EM reveals how VIPP1 oligomerizes, hydrolyzes nucleotides, and binds lipids•Lipid binding by VIPP1’s H1 helix maintains thylakoid integrity under high-light stress•VIPP1 coats mediate contact between thylakoids and the chloroplast envelope•VIPP1 is the photosynthetic homolog of ESCRT-III membrane-remodeling proteins Structure-function analysis and in situ visualization of VIPP1 provide insights into how this ESCRT-III homolog manipulates membranes to support thylakoid biogenesis and maintenance in cyanobacteria, algae, and plants.