Structural organisation of phycobilisomes from Synechocystis sp strain PCC6803 and their interaction with the membrane
| Autor: | Ghada Ajlani, Ana A. Arteni, Egbert J. Boekema |
|---|---|
| Přispěvatelé: | Electron Microscopy, Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS) |
| Jazyk: | angličtina |
| Rok vydání: | 2009 |
| Předmět: |
PORPHYRIDIUM-CRUENTUM
Photosystem II Biophysics Negative staining Biology Photosynthesis Cyanobacteria Models Biological Biochemistry NADP oxidoreductase PHOTOSYSTEM-II Phycocyanin Phycobilisomes Electron microscopy MOLECULAR CHARACTERIZATION WILD-TYPE Ferredoxin 3-DIMENSIONAL STRUCTURE Allophycocyanin Orange carotenoid protein Single particle image analysis Phycobiliprotein PARTICLE ELECTRON CRYOMICROSCOPY Cell Membrane Synechocystis PHYCOCYANIN-LESS MUTANT Cell Biology CYANOBACTERIAL PHYCOBILISOMES CRYSTAL-STRUCTURE ANALYSIS [SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriology Phycobilisome Ferredoxin-NADP Reductase Crystallography GLOEOBACTER-VIOLACEUS Mutation Peptides |
| Zdroj: | Biochimica et Biophysica Acta, 1787(4), 272-279 Biochimica biophysica acta (BBA)-Bioenergetics Biochimica biophysica acta (BBA)-Bioenergetics, 2009, 1787 (4), pp.272-279. ⟨10.1016/j.bbabio.2009.01.009⟩ |
| ISSN: | 0005-2728 1879-2650 |
| DOI: | 10.1016/j.bbabio.2009.01.009⟩ |
| Popis: | In cyanobacteria, the harvesting of light energy for photosynthesis is mainly carried out by the phycobilisome a giant, multi-subunit pigment-protein complex. This complex is composed of heterodimeric phycobiliproteins that are assembled with the aid of linker polypeptides such that light absorption and energy transfer to photosystem II are optimised. In this work we have studied, using single particle electron microscopy, the phycobilisome structure in mutants lacking either two or all three of the phycocyanin hexamers. The images presented give much greater detail than those previously published, and in the best two-dimensional projection maps a resolution of 13 angstrom was achieved. As well as giving a better overall picture of the assembly of phycobilisomes, these results reveal new details of the association of allophycocyanin trimers within the core. Insights are gained into the attachment of this core to the membrane surface, essential for efficient energy transfer to photosystem II. Comparison of projection maps of phycobilisomes with and without reconstituted ferredoxin:NADP oxidoreductase suggests a location for this enzyme within the complex at the rod-core interface. (C) 2009 Elsevier B.V. All rights reserved. |
| Databáze: | OpenAIRE |
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