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  Curvature thylakoid 1 proteins modulate prolamellar body morphology and promote organized thylakoid biogenesis in Arabidopsis thaliana

Sandoval-Ibanez, O., Sharma, A., Bykowski, M., Borràs-Gas, G., Behrendorff, J. B. Y. H., Mellor, S., et al. (2021). Curvature thylakoid 1 proteins modulate prolamellar body morphology and promote organized thylakoid biogenesis in Arabidopsis thaliana. Proceedings of the National Academy of Sciences of the United States of America, 118(42): e2113934118. doi:10.1073/pnas.2113934118.

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Sandoval-Ibanez, O.1, Author           
Sharma, Anurag2, Author
Bykowski, Michał2, Author
Borràs-Gas, Guillem2, Author
Behrendorff, James B. Y. H.2, Author
Mellor, Silas2, Author
Qvortrup, Klaus2, Author
Verdonk, Julian C.2, Author
Bock, R.1, Author           
Kowalewska, Łucja2, Author
Pribil, Mathias2, Author
1Organelle Biology and Biotechnology, Department Bock, Max Planck Institute of Molecular Plant Physiology, Max Planck Society, ou_1753326              
2External Organizations, ou_persistent22              


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 Abstract: Chloroplast biogenesis is a fundamental process occurring during seedling ontogenesis and leading to plant autotrophy. Which membrane components sterically organize the light-triggered transition of etioplast prolamellar bodies (PLBs) into chloroplast thylakoids, and thus mediate cubic–}lamellar transformation, is poorly understood. Here, we used combined two- and three-dimensional electron microscopy, spectroscopy, and biochemical methods to determine the role of CURT1 proteins in the formation of etioplast cubic membranes and their transformation to photosynthetically active chloroplast thylakoids. CURT1 proteins were previously recognized as significant contributors to thylakoid membrane folding. We found that CURT1 proteins are integral proteins of etioplast membranes and act as factors modulating PLBs and prothylakoid nanomorphology. They are also required for concerted thylakoid maturation under de-etiolation.The term {“}de-etiolation{”} refers to the light-dependent differentiation of etioplasts to chloroplasts in angiosperms. The underlying process involves reorganization of prolamellar bodies (PLBs) and prothylakoids into thylakoids, with concurrent changes in protein, lipid, and pigment composition, which together lead to the assembly of active photosynthetic complexes. Despite the highly conserved structure of PLBs among land plants, the processes that mediate PLB maintenance and their disassembly during de-etiolation are poorly understood. Among chloroplast thylakoid membrane{–localized proteins, to date, only Curvature thylakoid 1 (CURT1) proteins were shown to exhibit intrinsic membrane-bending capacity. Here, we show that CURT1 proteins, which play a critical role in grana margin architecture and thylakoid plasticity, also participate in de-etiolation and modulate PLB geometry and density. Lack of CURT1 proteins severely perturbs PLB organization and vesicle fusion, leading to reduced accumulation of the light-dependent enzyme protochlorophyllide oxidoreductase (LPOR) and a delay in the onset of photosynthesis. In contrast, overexpression of CURT1A induces excessive bending of PLB membranes, which upon illumination show retarded disassembly and concomitant overaccumulation of LPOR, though without affecting greening or the establishment of photosynthesis. We conclude that CURT1 proteins contribute to the maintenance of the paracrystalline PLB morphology and are necessary for efficient and organized thylakoid membrane maturation during de-etiolation.All study data are included in the article and/or SI Appendix and all raw data are available upon request from the corresponding authors.


Language(s): eng - English
 Dates: 2021
 Publication Status: Published in print
 Pages: -
 Publishing info: -
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 Rev. Type: -
 Identifiers: DOI: 10.1073/pnas.2113934118
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Title: Proceedings of the National Academy of Sciences of the United States of America
  Other : PNAS
  Other : Proceedings of the National Academy of Sciences of the USA
  Abbreviation : Proc. Natl. Acad. Sci. U. S. A.
Source Genre: Journal
Publ. Info: Washington, D.C. : National Academy of Sciences
Pages: - Volume / Issue: 118 (42) Sequence Number: e2113934118 Start / End Page: - Identifier: ISSN: 0027-8424
CoNE: https://pure.mpg.de/cone/journals/resource/954925427230