Heterogeneity in thylakoid membrane proteome of Synechocystis 6803

Agarwal, Renu; Matros, Andrea; Melzer, Michael; Mock, Hans‐Peter; Sainis, Jayashree Krishna

doi:10.1016/j.jprot.2009.12.011

Cited by 41 publications

(33 citation statements)

References 56 publications

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“…In intact thylakoid membranes within the cell, such PSIonly and PSI/PSII zones are expected to be contiguous, as seen in Figure 5 and Supplemental Figures 5, 8, 9, and 10. This is in line with previous evidence supporting some degree of spatial heterogeneity in cyanobacterial thylakoids (Vermaas et al, 2008;Sherman et al, 1994;Agarwal et al, 2010). The identification of PSI-rich membrane regions could have been anticipated, since PSI is the major photosystem in T. elongatus (PSI:PSII = 3.94); nevertheless, the existence of PSI-only membrane domains showing long-range order, and with no other membrane proteins such as Complex I present, was unexpected as no such arrangement has been seen previously despite extensive analyses of cyanobacterial thylakoid membranes by freeze-fracture and negative stain electron microscopy (Olive et al, 1986(Olive et al, , 1997Mörschel and Schatz, 1987;Vernotte et al, 1990;Westerman et al, 1994;Folea et al, 2008a).…”

Section: Discussionsupporting

confidence: 93%

Lateral Segregation of Photosystem I in Cyanobacterial Thylakoids

et al. 2017

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Photosystem I (PSI) is the dominant photosystem in cyanobacteria and it plays a pivotal role in cyanobacterial metabolism. Despite its biological importance, the native organization of PSI in cyanobacterial thylakoid membranes is poorly understood. Here, we use atomic force microscopy (AFM) to show that ordered, extensive macromolecular arrays of PSI complexes are present in thylakoids from Thermosynechococcus elongatus, Synechococcus sp PCC 7002, and Synechocystis sp PCC 6803. Hyperspectral confocal fluorescence microscopy and three-dimensional structured illumination microscopy of Synechocystis sp PCC 6803 cells visualize PSI domains within the context of the complete thylakoid system. Crystallographic and AFM data were used to build a structural model of a membrane landscape comprising 96 PSI trimers and 27,648 chlorophyll a molecules. Rather than facilitating intertrimer energy transfer, the close associations between PSI primarily maximize packing efficiency; short-range interactions with Complex I and cytochrome b 6 f are excluded from these regions of the membrane, so PSI turnover is sustained by long-distance diffusion of the electron donors at the membrane surface. Elsewhere, PSI-photosystem II contact zones provide sites for docking phycobilisomes and the formation of megacomplexes. PSI-enriched domains in cyanobacteria might foreshadow the partitioning of PSI into stromal lamellae in plants, similarly sustained by long-distance diffusion of electron carriers.

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Section: Discussionsupporting

confidence: 93%

Lateral Segregation of Photosystem I in Cyanobacterial Thylakoids

et al. 2017

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“…2A). The identification of TM-containing proteins from soluble fraction is likely caused by inefficient precipitation of membranous vesicles from the soluble fraction, as previously discussed by us and others (11,28,30,31). If we include only two-or more-TM containing proteins, to exclude proteins with a signal peptide that were otherwise predicted by TMHMM as 1-TM containing, as the true TM-containing proteins, the number of uniquely identified TM-containing proteins can be reduced to 115 and 0 in the membrane and the soluble fractions, respectively, and 133 were from both fractions ( Fig.…”

Section: Fig 1 Rational and Experimental Designmentioning

confidence: 63%

“…The linear trend of the plot suggests that the two types of ratios correlate very well (R 2 ϭ 0.83) in representing the relative abundances of proteins in the membrane and the soluble fractions. In the plot, we included also the predicted TM-containing proteins that should have high M/S ratios because integral membrane proteins localize primarily on the membrane though some may localize on membranous vesicles that do not co-precipitate with membranes under the centrifugation condition we used (31). As expected, the majority of the two or more TM-containing proteins that are expected to be true IMPs distribute in the region 2 on the plot where proteins have high M/S ratios for both peptide spectral counts and peak intensities (Fig.…”

Section: Large-scale Ranking Of the Tightness Of The Association Betwmentioning

confidence: 99%

Systematically Ranking the Tightness of Membrane Association for Peripheral Membrane Proteins (PMPs) *

Gao

Huang

et al. 2015

Molecular & Cellular Proteomics

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Large-scale quantitative evaluation of the tightness of membrane association for nontransmembrane proteins is important for identifying true peripheral membrane proteins with functional significance. Herein, we simultaneously ranked more than 1000 proteins of the photosynthetic model organism Synechocystis sp. PCC 6803 for their relative tightness of membrane association using a proteomic approach. Using multiple precisely ranked and experimentally verified peripheral subunits of photosynthetic protein complexes as the landmarks, we found that proteins involved in two-component signal transduction systems and transporters are overall tightly associated with the membranes, whereas the associations of ribosomal proteins are much weaker. Moreover, we found that hypothetical proteins containing the same domains generally have similar tightness. This work provided a global view of the structural organization of the membrane proteome with respect to divergent functions, and built the foundation for future investigation of the dynamic membrane proteome reorganization in response to different environmental or internal stimuli. Molecular & Cellular Proteomics

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“…In the same study, ARTO was unable to oxidize plastoquinol in a COX/Cyd mutant, suggesting that it cannot substitute for Cyd in the thylakoid membrane. Proteomics studies on purified membrane fractions have confirmed the presence of the CtaCII subunit of ARTO in the cytoplasmic membrane (Huang et al, 2002(Huang et al, , 2006Pisareva et al, 2007) but not in the thylakoid membrane (Srivastava et al, 2005;Agarwal et al, 2010) of Synechocystis. However subunits of the other terminal oxidases were not identified in these same studies (Srivastava et al, 2005;Agarwal et al, 2010), suggesting that terminal oxidases are present in low abundance in both membranes.…”

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confidence: 99%

“…The purity of these membrane fractions was confirmed by probing with thylakoidand cytoplasmic membrane-specific antibodies. In addition, proteomic studies have detected cyt b 6 f subunits in purified thylakoid membrane fractions (Srivastava et al, 2005;Agarwal et al, 2010) but not in cytoplasmic membranes from Synechocystis cultured under normal (Huang et al, 2002) and salt-stressed (Huang et al, 2006) conditions. This suggests the presence of a simpler respiratory chain in the cytoplasmic membrane, in which electrons donated to plastoquinone by dehydrogenase complexes are transferred directly to plastoquinolreduced terminal oxidases.…”

mentioning

confidence: 99%

Thylakoid Terminal Oxidases Are Essential for the CyanobacteriumSynechocystissp. PCC 6803 to Survive Rapidly Changing Light Intensities

et al. 2013

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Cyanobacteria perform photosynthesis and respiration in the thylakoid membrane, suggesting that the two processes are interlinked. However, the role of the respiratory electron transfer chain under natural environmental conditions has not been established. Through targeted gene disruption, mutants of Synechocystis sp. PCC 6803 were generated that lacked combinations of the three terminal oxidases: the thylakoid membrane-localized cytochrome c oxidase (COX) and quinol oxidase (Cyd) and the cytoplasmic membrane-localized alternative respiratory terminal oxidase. All strains demonstrated similar growth under continuous moderate or high light or 12-h moderate-light/dark square-wave cycles. However, under 12-h high-light/dark square-wave cycles, the COX/Cyd mutant displayed impaired growth and was completely photobleached after approximately 2 d. In contrast, use of sinusoidal light/dark cycles to simulate natural diurnal conditions resulted in little photobleaching, although growth was slower. Under high-light/dark square-wave cycles, the COX/Cyd mutant suffered a significant loss of photosynthetic efficiency during dark periods, a greater level of oxidative stress, and reduced glycogen degradation compared with the wild type. The mutant was susceptible to photoinhibition under pulsing but not constant light. These findings confirm a role for thylakoid-localized terminal oxidases in efficient dark respiration, reduction of oxidative stress, and accommodation of sudden light changes, demonstrating the strong selective pressure to maintain linked photosynthetic and respiratory electron chains within the thylakoid membrane. To our knowledge, this study is the first to report a phenotypic difference in growth between terminal oxidase mutants and wild-type cells and highlights the need to examine mutant phenotypes under a range of conditions.

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Heterogeneity in thylakoid membrane proteome of Synechocystis 6803

Cited by 41 publications

References 56 publications

Lateral Segregation of Photosystem I in Cyanobacterial Thylakoids

Lateral Segregation of Photosystem I in Cyanobacterial Thylakoids

Systematically Ranking the Tightness of Membrane Association for Peripheral Membrane Proteins (PMPs) *

Thylakoid Terminal Oxidases Are Essential for the CyanobacteriumSynechocystissp. PCC 6803 to Survive Rapidly Changing Light Intensities

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