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The Structure of Photosystem II in Arabidopsis: Localization of the CP26 and CP29 Antenna Complexes†
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and Peter Horton*
Section:Abstract
A genetic approach has been adopted to investigate the organization of the light-harvesting proteins in the photosystem II (PSII) complex in plants. PSII membrane fragments were prepared from wild-type Arabidopis thaliana and plants expressing antisense constructs to Lhcb4 and Lhcb5 genes, lacking CP29 and CP26, respectively (Andersson et al. (2001) Plant Cell 13, 1193−1204). Ordered PS II arrays and PS II supercomplexes were isolated from the membranes of plants lacking CP26 but could not be prepared from those lacking CP29. Membranes and supercomplexes lacking CP26 were less stable than those prepared from the wild type. Transmission electron microscopy aided by single-particle image analysis was applied to the ordered arrays and the isolated PSII complexes. The difference between the images obtained from wild type and antisense plants showed the location of CP26 to be near CP43 and one of the light-harvesting complex trimers. Therefore, the location of the CP26 within PSII was directly established for the first time, and the location of the CP29 complex was determined by elimination. Alterations in the packing of the PSII complexes in the thylakoid membrane also resulted from the absence of CP26. The minor light-harvesting complexes each have a unique location and important roles in the stabilization of the oligomeric PSII structure.
Citing Articles
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This article has been cited by 5 ACS Journal articles (5 most recent appear below).
Phosphorylation of Photosynthetic Antenna Protein CP29 and Photosystem II Structure Changes in Monocotyledonous Plants under Environmental Stresses
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Yang-Er Chen, Shu Yuan, Jun-Bo Du, Mo-Yun Xu, Zhong-Wei Zhang and Hong-Hui LinBiochemistry2009 48 (41), 9757-9763Kinetic studies of protein dephosphorylation in thylakoid membranes showed that the minor light-harvesting antenna protein CP29 could be phosphorylated in barley (C3) and maize (C4) seedlings, but not in spinach under water [Liu, W. J., et al. (2009) ...
Intrinsically Unstructured Phosphoprotein TSP9 Regulates Light Harvesting in Arabidopsis thaliana
Rikard Fristedt, Inger Carlberg, Agnieszka Zygadlo, Mirva Piippo, Markus Nurmi, Eva-Mari Aro, Henrik Vibe Scheller and Alexander V. VenerBiochemistry2009 48 (2), 499-509Intrinsically Unstructured Phosphoprotein TSP9 Regulates Light Harvesting in Arabidopsis thaliana
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Micelle-Induced Folding of Spinach Thylakoid Soluble Phosphoprotein of 9 kDa and Its Functional Implications,
Jikui Song, Min S. Lee, Inger Carlberg, Alexander V. Vener, and John L. MarkleyBiochemistry2006 45 (51), 15633-15643Micelle-Induced Folding of Spinach Thylakoid Soluble Phosphoprotein of 9 kDa and Its Functional Implications,
Jikui Song, Min S. Lee, Inger Carlberg, Alexander V. Vener, and John L. MarkleyBiochemistry2006 45 (51), 15633-15643Thylakoid soluble phosphoprotein of 9 kDa (TSP9) has been identified as a plant-specific protein in the photosynthetic thylakoid membrane (Carlberg et al. (2003) Proc. Natl. Acad. Sci. 100, 757−762). Nonphosphorylated TSP9 is associated with the membrane, ...
Photophysical Behavior and Assignment of the Low-Energy Chlorophyll States in the CP43 Proximal Antenna Protein of Higher Plant Photosystem II
Joseph L. Hughes, Rafael Picorel, Michael Seibert, and Elmars KrauszBiochemistry2006 45 (40), 12345-12357Photophysical Behavior and Assignment of the Low-Energy Chlorophyll States in the CP43 Proximal Antenna Protein of Higher Plant Photosystem II
Joseph L. Hughes, Rafael Picorel, Michael Seibert, and Elmars KrauszBiochemistry2006 45 (40), 12345-12357We have employed absorption, circular dichroism (CD), and persistent spectral hole-burning measurements at 1.7 K to study the photoconversion properties and exciton coupling of low-energy chlorophylls (Chls) in the CP43 proximal antenna light-harvesting ...
Structure of the Higher Plant Light Harvesting Complex I: In Vivo Characterization and Structural Interdependence of the Lhca Proteins
Frank Klimmek, Ulrika Ganeteg, Janne A. Ihalainen, Henny van Roon, Poul E. Jensen, Henrik V. Scheller, Jan P. Dekker, and Stefan JanssonBiochemistry2005 44 (8), 3065-3073Structure of the Higher Plant Light Harvesting Complex I: In Vivo Characterization and Structural Interdependence of the Lhca Proteins
Frank Klimmek, Ulrika Ganeteg, Janne A. Ihalainen, Henny van Roon, Poul E. Jensen, Henrik V. Scheller, Jan P. Dekker, and Stefan JanssonBiochemistry2005 44 (8), 3065-3073We have investigated the structure of the higher plant light harvesting complex of photosystem I (LHCI) by analyzing PSI−LHCI particles isolated from a set of Arabidopsis plant lines, each lacking a specific Lhca (Lhca1−4) polypeptide. Functional antenna ...
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History
- Published In Issue January 28, 2003
- Received November 4, 2002
Revised Manuscript Received December 2, 2002
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