Chloroplast structure: from chlorophyll granules to supra-molecular architecture of thylakoid membranes

Staehelin, L. Andrew

doi:10.1007/1-4020-3324-9_64

Cited by 62 publications

(76 citation statements)

References 45 publications

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“…The PFs fracture face containing LHCII particles is complementary to the EFs PSII fracture face (Simpson, 1979;Staehelin, 2003). There was a noticeable increase in the packing of LHCII complexes on the PFs fracture faces in the Light Zea chloroplasts ( Figure 3C, arrow 2) compared with the Dark Vio chloroplasts ( Figure 3A).…”

Section: The Photoprotective Structural Change Remodels the Psii-lhcimentioning

confidence: 97%

“…The freeze-fracture technique splits hydrophobic core of the membrane bilayer into the exoplasmic and protoplasmic leaflets, allowing information on the organization and dimensions of the proteins therein to be determined by image analysis. Four distinct fracture faces are observed in freeze-fracture EM images (reviewed in Staehelin, 2003) (Figure 2A). The exoplasmic fracture face of the stacked membranes (EFs) is dominated by PSII particles of ;16 to 18 nm (Staehelin, 1976;Armond et al, 1977).…”

Section: The Photoprotective Structural Change Remodels the Psii-lhcimentioning

confidence: 99%

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Photoprotective Energy Dissipation Involves the Reorganization of Photosystem II Light-Harvesting Complexes in the Grana Membranes of Spinach Chloroplasts

et al. 2011

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Plants must regulate their use of absorbed light energy on a minute-by-minute basis to maximize the efficiency of photosynthesis and to protect photosystem II (PSII) reaction centers from photooxidative damage. The regulation of light harvesting involves the photoprotective dissipation of excess absorbed light energy in the light-harvesting antenna complexes (LHCs) as heat. Here, we report an investigation into the structural basis of light-harvesting regulation in intact spinach (Spinacia oleracea) chloroplasts using freeze-fracture electron microscopy, combined with laser confocal microscopy employing the fluorescence recovery after photobleaching technique. The results demonstrate that formation of the photoprotective state requires a structural reorganization of the photosynthetic membrane involving dissociation of LHCII from PSII and its aggregation. The structural changes are manifested by a reduced mobility of LHC antenna chlorophyll proteins. It is demonstrated that these changes occur rapidly and reversibly within 5 min of illumination and dark relaxation, are dependent on DpH, and are enhanced by the deepoxidation of violaxanthin to zeaxanthin.

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Section: The Photoprotective Structural Change Remodels the Psii-lhcimentioning

confidence: 97%

Section: The Photoprotective Structural Change Remodels the Psii-lhcimentioning

confidence: 99%

Photoprotective Energy Dissipation Involves the Reorganization of Photosystem II Light-Harvesting Complexes in the Grana Membranes of Spinach Chloroplasts

et al. 2011

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“…To compare the PG proteomes with prolamellar bodies (Staehelin, 2003) and possibly PGs in etioplasts, we grew rice (Oryza sativa) seedlings in complete darkness and purified the etioplasts. We then used the PG purification procedure to collect low-density lipid particles and membranes from these etioplasts.…”

Section: Purification and Identification Of The Proteome Of Low-densimentioning

confidence: 99%

Protein Profiling of Plastoglobules in Chloroplasts and Chromoplasts. A Surprising Site for Differential Accumulation of Metabolic Enzymes

2006

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Plastoglobules (PGs) are oval or tubular lipid-rich structures present in all plastid types, but their specific functions are unclear. PGs contain quinones, a-tocopherol, and lipids and, in chromoplasts, carotenoids as well. It is not known whether PGs contain any enzymes or regulatory proteins. Here, we determined the proteome of PGs from chloroplasts of stressed and unstressed leaves of Arabidopsis (Arabidopsis thaliana) as well as from pepper (Capsicum annuum) fruit chromoplasts using mass spectrometry. Together, this showed that the proteome of chloroplast PGs consists of seven fibrillins, providing a protein coat and preventing coalescence of the PGs, and an additional 25 proteins likely involved in metabolism of isoprenoid-derived molecules (quinines and tocochromanols), lipids, and carotenoid cleavage. Four unknown ABC1 kinases were identified, possibly involved in regulation of quinone monooxygenases. Most proteins have not been observed earlier but have predicted N-terminal chloroplast transit peptides and lack transmembrane domains, consistent with localization in the PG lipid monolayer particles. Quantitative differences in PG composition in response to high light stress and degreening were determined by differential stable-isotope labeling using formaldehyde. More than 20 proteins were identified in the PG proteome of pepper chromoplasts, including four enzymes of carotenoid biosynthesis and several homologs of proteins observed in the chloroplast PGs. Our data strongly suggest that PGs in chloroplasts form a functional metabolic link between the inner envelope and thylakoid membranes and play a role in breakdown of carotenoids and oxidative stress defense, whereas PGs in chromoplasts are also an active site for carotenoid conversions.

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“…Whereas the evidence for trimeric arrangements of PSI in vivo is scarce, there is evidence for a functionally relevant distinction between PSII monomers and dimers from freeze-fracture analysis of plant thylakoids: PSII dimers are in grana regions and PSII monomers are in unstacked thylakoid regions [31,32]. As PSII in unstacked regions of the plant thylakoid may correspond to photosystems that are undergoing repair [33,34], the interchange between monomeric and dimeric PSII complexes in the membrane indeed may be rapid.…”

Section: Turnover Of Psii and Psi Proteinsmentioning

confidence: 99%

Lifetimes of photosystem I and II proteins in the cyanobacterium Synechocystis sp. PCC 6803

2011

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Edited by Richard CogdellKeywords: Photosystem I Photosystem II Small Cab-like protein Protein turnover Half-life time a b s t r a c tThe half-life times of photosystem I and II proteins were determined using 15 N-labeling and mass spectrometry. The half-life times (30-75 h for photosystem I components and <1-11 h for the large photosystem II proteins) were similar when proteins were isolated from monomeric vs. oligomeric complexes on Blue-Native gels, suggesting that the two forms of both photosystems can interchange on a timescale of <1 h or that only one form of each photosystem exists in thylakoids in vivo. The half-life times of proteins associated with either photosystem generally were unaffected by the absence of Small Cab-like proteins.

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Chloroplast structure: from chlorophyll granules to supra-molecular architecture of thylakoid membranes

Cited by 62 publications

References 45 publications

Photoprotective Energy Dissipation Involves the Reorganization of Photosystem II Light-Harvesting Complexes in the Grana Membranes of Spinach Chloroplasts

Photoprotective Energy Dissipation Involves the Reorganization of Photosystem II Light-Harvesting Complexes in the Grana Membranes of Spinach Chloroplasts

Protein Profiling of Plastoglobules in Chloroplasts and Chromoplasts. A Surprising Site for Differential Accumulation of Metabolic Enzymes

Lifetimes of photosystem I and II proteins in the cyanobacterium Synechocystis sp. PCC 6803

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