NDLI: Arabidopsis CURVATURE THYLAKOID1 Proteins Modify Thylakoid Architecture by Inducing Membrane Curvature

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Armbruster, Ute Labs, Mathias Pribil, Mathias Viola, Stefania Xu, Wenteng Scharfenberg, Michael Hertle, Alexander P. Rojahn, Ulrike Jensen, Poul Erik Rappaport, Fabrice Joliot, Pierre Dörmann, Peter Wanner, Gerhard Leister, Dario
Description	Country affiliation: Germany Author Affiliation: Armbruster U ( Plant Molecular Biology (Botany), Department Biology I, Ludwig-Maximilians-Universität München, 81252 Planegg-Martinsried, Germany.)
Abstract	Chloroplasts of land plants characteristically contain grana, cylindrical stacks of thylakoid membranes. A granum consists of a core of appressed membranes, two stroma-exposed end membranes, and margins, which connect pairs of grana membranes at their lumenal sides. Multiple forces contribute to grana stacking, but it is not known how the extreme curvature at margins is generated and maintained. We report the identification of the CURVATURE THYLAKOID1 (CURT1) protein family, conserved in plants and cyanobacteria. The four Arabidopsis thaliana CURT1 proteins (CURT1A, B, C, and D) oligomerize and are highly enriched at grana margins. Grana architecture is correlated with the CURT1 protein level, ranging from flat lobe-like thylakoids with considerably fewer grana margins in plants without CURT1 proteins to an increased number of membrane layers (and margins) in grana at the expense of grana diameter in overexpressors of CURT1A. The endogenous CURT1 protein in the cyanobacterium Synechocystis sp PCC6803 can be partially replaced by its Arabidopsis counterpart, indicating that the function of CURT1 proteins is evolutionary conserved. In vitro, Arabidopsis CURT1A proteins oligomerize and induce tubulation of liposomes, implying that CURT1 proteins suffice to induce membrane curvature. We therefore propose that CURT1 proteins modify thylakoid architecture by inducing membrane curvature at grana margins.
File Format	HTM / HTML
ISSN	10404651
e-ISSN	1531298X
DOI	10.1105/tpc.113.113118
Journal	THE PLANT CELL ONLINE
Issue Number	7
Volume Number	25
Language	English
Publisher	American Society of Plant Biologists
Publisher Date	2013-07-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Discipline Botany Arabidopsis Proteins Metabolism Chloroplasts Intracellular Membranes Thylakoids Amino Acid Sequence Arabidopsis Genetics Classification Chlorophyll Ultrastructure Immunoblotting Lipids Microscopy, Electron, Scanning Microscopy, Electron, Transmission Molecular Sequence Data Mutation Phosphorylation Photosynthesis Phylogeny Proteolipids Reverse Transcriptase Polymerase Chain Reaction Sequence Homology, Amino Acid Research Support, Non-u.s. Gov't
Content Type	Text
Resource Type	Article
Subject	Cell Biology Plant Science

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