Proteomics of Synechocystis sp. Strain PCC 6803

Huang, Fang; Parmryd, Ingela; Nilsson, Fred; Persson, Anna; Pakrasi, Himadri B.; Andersson, Bertil; Norling, Birgitta

doi:10.1074/mcp.m200043-mcp200

Cited by 162 publications

(85 citation statements)

References 75 publications

(77 reference statements)

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“…For example, in this organism ZnuA has a transmembrane ␣-helix, whereas MntC is tethered via a lipid anchor (5,6). FutA1 is a predicted lipoprotein (41,42), although there has been some debate about its association with thylakoid versus plasma membranes (43,44). Crucially, FutA1 has never been observed in soluble periplasmic extracts (40,43).…”

Section: Discussionmentioning

confidence: 99%

A Periplasmic Iron-binding Protein Contributes toward Inward Copper Supply

Waldron¹,

Tottey²,

Yanagisawa

et al. 2007

Journal of Biological Chemistry

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Periplasmic substrate binding proteins are known for iron, zinc, manganese, nickel, and molybdenum but not copper. Synechocystis PCC 6803 requires copper for thylakoid-localized plastocyanin and cytochrome oxidase. Here we show that mutants deficient in a periplasmic substrate binding protein FutA2 have low cytochrome oxidase activity and produce cytochrome c 6 when grown under copper conditions (150 nM) in which wild-type cells use plastocyanin rather than cytochrome c 6 . Anaerobic separation of extracts by two-dimensional native liquid chromatography followed by metal analysis and peptide mass-fingerprinting establish that accumulation of copperplastocyanin is impaired, but iron-ferredoxin is unaffected in ⌬futA2 grown in 150 nM copper. However, recombinant FutA2 binds iron in preference to copper in vitro with an apparent Fe(III) affinity similar to that of its paralog FutA1, the principal substrate binding protein for iron import. FutA2 is also associated with iron and not copper in periplasm extracts, and this Fe(III)-protein complex is absent in ⌬futA2. There are differences in the soluble protein and small-molecule complexes of copper and iron, and the total amount of both elements increases in periplasm extracts of ⌬futA2 relative to wild type. Changes in periplasm protein and small-molecule complexes for other metals are also observed in ⌬futA2. It is proposed that FutA2 contributes to metal partitioning in the periplasm by sequestering Fe(III), which limits aberrant Fe(III) associations with vital binding sites for other metals, including copper.Oxygenic phototrophs have exceptional requirements for metals such as iron, copper, and manganese within the photosynthetic machinery (1, 2). There is interest in understanding how metal ions partition to the correct cellular destinations in all organisms (3), including to the approximately one-third of proteins that need metals (4). The periplasm is a key location for metal partitioning. Bacterial ATP binding cassette (ABC)-type importers include substrate binding proteins which may be free within the periplasm or anchored to the outer face of the plasma membrane. It is anticipated that these proteins assist in loading metal ions onto the correct importers. There is similarity in the metal-binding sites of several substrate binding proteins that contribute toward the import of distinct metals, such as manganese versus zinc, and subtle differences in second coordination spheres may be crucial for metal selectivity (5). It has also been noted that the nature of interactions between substrate binding proteins and their respective metal transporters may make a key contribution to metal specificity (5

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Section: Discussionmentioning

confidence: 99%

A Periplasmic Iron-binding Protein Contributes toward Inward Copper Supply

Waldron¹,

Tottey²,

Yanagisawa

et al. 2007

Journal of Biological Chemistry

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“…PCC6803 as a start point, but expressing this as a membrane protein in E. coli for which there were no identified orthologues. The protein has an undetermined function but has been identified in the plasma membrane of Synechocystis [43], with the predicted gene product consisting of 673 amino acids with a single predicted transmembrane alphahelix close to the N-terminus. A portion of the sll1021 sequence coding for 38 amino acids including the predicted transmembrane alpha-helix was fused in-frame to the gene coding for GFPmut3* [44] with a linker of five asparagine residues.…”

Section: Materials and Methods (A) Bacterial Cell Strain And Preparationmentioning

confidence: 99%

Inferring diffusion in single live cells at the single-molecule level

Robson

Burrage

Leake

2013

Phil. Trans. R. Soc. B

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The movement of molecules inside living cells is a fundamental feature of biological processes. The ability to both observe and analyse the details of molecular diffusion in vivo at the single-molecule and single-cell level can add significant insight into understanding molecular architectures of diffusing molecules and the nanoscale environment in which the molecules diffuse. The tool of choice for monitoring dynamic molecular localization in live cells is fluorescence microscopy, especially so combining total internal reflection fluorescence with the use of fluorescent protein (FP) reporters in offering exceptional imaging contrast for dynamic processes in the cell membrane under relatively physiological conditions compared with competing single-molecule techniques. There exist several different complex modes of diffusion, and discriminating these from each other is challenging at the molecular level owing to underlying stochastic behaviour. Analysis is traditionally performed using mean square displacements of tracked particles; however, this generally requires more data points than is typical for single FP tracks owing to photophysical instability. Presented here is a novel approach allowing robust Bayesian ranking of diffusion processes to discriminate multiple complex modes probabilistically. It is a computational approach that biologists can use to understand single-molecule features in live cells.

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“…Mackey et al (2013) and Pittera et al (2014) have shown a similar decrease in D1 protein expression in tropical isolates at low temperatures correlating with lower growth rate. D1 is sensitive to environmental stress and susceptible to photo-oxidative damage and requires replacement through a continuous repair cycle for the maintenance of photosynthesis (Huang et al, 2002). In freshwater cyanobacteria, to overcome low temperature-induced inhibition of the repair cycle, increased membrane fluidity and de novo protein synthesis are required (Kanervo et al, 1997;Suzuki et al, 2001;Murata et al, 2007;Tyystjärvi et al, 2001).…”

Section: Molecular-level Adaptations To Growth Temperaturementioning

confidence: 99%

Effects of low temperature on tropical and temperate isolates of marine Synechococcus

et al. 2015

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Temperature is an important factor influencing the distribution of marine picocyanobacteria. However, molecular responses contributing to temperature preferences are poorly understood in these important primary producers. We compared the temperature acclimation of a tropical Synechococcus strain WH8102 with temperate strain BL107 at 18°C relative to 22°C and examined their global protein expression, growth patterns, photosynthetic efficiency and lipid composition.Global protein expression profiles demonstrate the partitioning of the proteome into major categories: photosynthesis (440%), translation (10-15%) and membrane transport (2-8%) with distinct differences between and within strains grown at different temperatures. At low temperature, growth and photosynthesis of strain WH8102 was significantly decreased, while BL107 was largely unaffected. There was an increased abundance of proteins involved in protein biosynthesis at 18°C for BL107. Each strain showed distinct differences in lipid composition with higher unsaturation in strain BL107. We hypothesize that differences in membrane fluidity, abundance of protein biosynthesis machinery and the maintenance of photosynthesis efficiency contribute to the acclimation of strain BL107 to low temperature. Additional proteins unique to BL107 may also contribute to this strain's improved fitness at low temperature. Such adaptive capacities are likely important factors favoring growth of temperate strains over tropical strains in high latitude niches.

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Proteomics of Synechocystis sp. Strain PCC 6803

Cited by 162 publications

References 75 publications

A Periplasmic Iron-binding Protein Contributes toward Inward Copper Supply

A Periplasmic Iron-binding Protein Contributes toward Inward Copper Supply

Inferring diffusion in single live cells at the single-molecule level

Effects of low temperature on tropical and temperate isolates of marine Synechococcus

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