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TitleStructural basis for VIPP1 oligomerization and maintenance of thylakoid membrane integrity.
Journal, issue, pagesCell, Vol. 184, Issue 14, Page 3643-3659.e23, Year 2021
Publish dateJul 8, 2021
AuthorsTilak Kumar Gupta / Sven Klumpe / Karin Gries / Steffen Heinz / Wojciech Wietrzynski / Norikazu Ohnishi / Justus Niemeyer / Benjamin Spaniol / Miroslava Schaffer / Anna Rast / Matthias Ostermeier / Mike Strauss / Jürgen M Plitzko / Wolfgang Baumeister / Till Rudack / Wataru Sakamoto / Jörg Nickelsen / Jan M Schuller / Michael Schroda / Benjamin D Engel /
PubMed AbstractVesicle-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 ...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.
External linksCell / PubMed:34166613
MethodsEM (tomography) / EM (single particle)
Resolution3.8 - 5.0 Å
Structure data

EMDB-12324:
In situ cryo-electron tomogram of the Synechocystis wild-type VIPP1 strain grown in high light
Method: EM (tomography)

EMDB-12325:
In situ cryo-electron tomogram of the Synechocystis F4E VIPP1 mutant grown in high light
Method: EM (tomography)

EMDB-12326:
In situ cryo-electron tomogram of the Synechocystis V11E VIPP1 mutant grown in high light
Method: EM (tomography)

EMDB-12327:
In situ cryo-electron tomogram of a cluster of VIPP1-mCherry structures inside the Chlamydomonas chloroplast
Method: EM (tomography)

EMDB-12328:
In situ cryo-electron tomogram of a cluster of VIPP1-mCherry structures inside the Chlamydomonas chloroplast
Method: EM (tomography)

EMDB-12329:
In situ cryo-electron tomogram of a cluster of VIPP1-mCherry structures inside the Chlamydomonas chloroplast
Method: EM (tomography)

EMDB-12330:
In situ cryo-electron tomogram of a cluster of VIPP1-mCherry structures inside the Chlamydomonas chloroplast
Method: EM (tomography)

12710

7o3w

EMDB-12710, PDB-7o3w:
Structural basis for VIPP1 oligomerization and maintenance of thylakoid membrane integrity
Method: EM (single particle) / Resolution: 4.9 Å

12711

7o3x

EMDB-12711, PDB-7o3x:
Structural basis for VIPP1 oligomerization and maintenance of thylakoid membrane integrity
Method: EM (single particle) / Resolution: 3.9 Å

12712

7o3y

EMDB-12712, PDB-7o3y:
Structural basis for VIPP1 oligomerization and maintenance of thylakoid membrane integrity
Method: EM (single particle) / Resolution: 3.8 Å

12713

7o40

EMDB-12713, PDB-7o40:
Structural basis for VIPP1 oligomerization and maintenance of thylakoid membrane integrity
Method: EM (single particle) / Resolution: 4.3 Å

12714

7o3z

EMDB-12714, PDB-7o3z:
Structural basis for VIPP1 oligomerization and maintenance of thylakoid membrane integrity
Method: EM (single particle) / Resolution: 5.0 Å

Chemicals

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM / Adenosine diphosphate

Source
  • Synechocystis sp. PCC 6803 (bacteria)
  • Chlamydomonas reinhardtii (plant)
  • synechocystis sp. (strain pcc 6803 / kazusa) (bacteria)
KeywordsLIPID BINDING PROTEIN / ESCRT-III / Membrane remodelling / nucleotide hydrolysis / photosynthesis / thylakoid biogenesis / stress response

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