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  • 1
    Publication Date: 2023-01-30
    Keywords: Arabian Sea; Calculated; CD132; CD132 _AMBITION; CD132_AMBITION/1; CD132_AMBITION/2; CD132_AMBITION/3; CD132_AMBITION/4; CD132/1; CD132/2; CD132/3; CD132/4; Charles Darwin; CTD, Seabird; CTD-R; Date/Time of event; DEPTH, water; Diazotrophs, total biomass as carbon; Event label; Fluorescence-based quantitative real-time PCR (qPCR); Latitude of event; Longitude of event; MAREDAT_Diazotrophs_Collection; Unicellular cyanobacteria, biomass; Unicellular cyanobacteria-B, abundance expressed in number of nifH gene copies; Unicellular cyanobacteria-B, biological trait, ratio expressed in mass of carbon per amount of nifH gene copies
    Type: Dataset
    Format: text/tab-separated-values, 96 data points
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  • 2
    Publication Date: 2022-05-26
    Description: © The International Society for Microbial Ecology, 2015. This article is distributed under the terms of the Creative Commons Attribution License. The definitive version was published in ISME Journal 10 (2016): 968–978, doi:10.1038/ismej.2015.172.
    Description: Upon phosphorus (P) deficiency, marine phytoplankton reduce their requirements for P by replacing membrane phospholipids with alternative non-phosphorus lipids. It was very recently demonstrated that a SAR11 isolate also shares this capability when phosphate starved in culture. Yet, the extent to which this process occurs in other marine heterotrophic bacteria and in the natural environment is unknown. Here, we demonstrate that the substitution of membrane phospholipids for a variety of non-phosphorus lipids is a conserved response to P deficiency among phylogenetically diverse marine heterotrophic bacteria, including members of the Alphaproteobacteria and Flavobacteria. By deletion mutagenesis and complementation in the model marine bacterium Phaeobacter sp. MED193 and heterologous expression in recombinant Escherichia coli, we confirm the roles of a phospholipase C (PlcP) and a glycosyltransferase in lipid remodelling. Analyses of the Global Ocean Sampling and Tara Oceans metagenome data sets demonstrate that PlcP is particularly abundant in areas characterized by low phosphate concentrations. Furthermore, we show that lipid remodelling occurs seasonally and responds to changing nutrient conditions in natural microbial communities from the Mediterranean Sea. Together, our results point to the key role of lipid substitution as an adaptive strategy enabling heterotrophic bacteria to thrive in the vast P-depleted areas of the ocean.
    Description: This work was partially supported by grants STORM (CTM2009-09352/MAR), MALASPINA (CSD2008-00077), HOTMIX (CTM2011-30010/MAR), DOREMI (CTM2012-34294) and EcoBGM (CTM2013-48292-C3-3-R) funded by the Spanish Government, GAČR project GA13-11281S and MESOAQUA (228224) funded by the European Union Seventh Framework Program (FP7/2007-2013) and by the Natural Environment Research Council (NERC), UK (NE/M002233/1).
    Repository Name: Woods Hole Open Access Server
    Type: Article
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  • 3
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract An oligomer probe was designed to detect the presence of a putative phoB gene in the genome of the marine, phycoerythrincontaining cyanobacterium Synechococcus sp. WH7803. A 2.2 kb PstI fragment, identified using this probe, was cloned and the complete nucleotide sequence determined. The fragment contained two open reading frames encoding polypeptides which display all the sequence features expected of the response regulator and histidine protein kinase elements of a two component sensory system. Northern analysis confirmed that transcription of these genes was induced by phosphate limitation. On the basis of the sequence similarities and the regulation of their transcription by the availability of inorganic phosphate (Pi) these open reading frames were designated as phoB and phoR, respectively.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract The region of the genome encoding the glucose-6-phosphate dehydrogenase gene zwf was analysed in a unicellular cyanobacterium, Synechococcus sp. PCC 7942, and a filamentous, heterocystous cyanobacterium, Anabaena sp. PCC 7120. Comparison of cyanobacterial zwf sequences revealed the presence of two absolutely conserved cysteine residues which may be implicated in the light/dark control of enzyme activity. The presence in both strains of a gene fbp, encoding fructose-1,6-bisphosphatase, upstream from zwf strongly suggests that the oxidative pentose phosphate pathway in these organisms may function to completely oxidize glucose 6-phosphate to CO2. The amino acid sequence of fructose-1,6-bisphosphatase does not support the idea of its light activation by a thiol/disulfide exchange mechanism. In the case of Anabaena sp. PCC 7120, the tal gene, encoding transaldolase, lies between zwf and fbp.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology ecology 40 (2002), S. 0 
    ISSN: 1574-6941
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Oxygenic photoautotrophs of the genera Synechococcus and Prochlorococcus contribute significantly to primary production and are now widely accepted as the most abundant members of the picophytoplankton in the world's oceans. Since they represent one of the few cultured and representative groups of marine microorganisms, study of their physiology and biochemistry has progressed rapidly since their discovery. The recent and on-going sequencing of the complete genomes of representative strains will further hasten our understanding, and allow a complete interrogation, of the metabolism of these organisms. Moreover, since they inhabit a relatively simple environment they provide an excellent model system to begin to identify the underlying molecular mechanisms which allow their success in water columns with large vertical gradients of light and nutrients. Such work should provide novel insights into the genetic adaptations of these important marine microbes to their environment. We review here molecular ecological methods that are already available or which are currently being developed for these organisms. Such methods allow community structure, growth rate and nutrient status analysis, potentially at the single cell level, and can be used to define the niches, or identify the biotic or abiotic factors, which might control the productivity of specific genotypes. These techniques will undoubtedly provide the tools for answering more discerning questions concerning their ecology. How the complete genome sequence information is providing insights, and can further facilitate our understanding, of the ecology of these organisms is also discussed.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Molecular microbiology 14 (1994), S. 0 
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
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  • 7
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: During phosphate-limited growth the marine phycoerythrin-containing picoplanktonic cyanobacterium Synechococcus sp. WH7803 synthesizes novel polypeptides, including two abundant species of 100 kDa and 32kDa. The 32kDa polypeptide was localized to the cell wall, although in a related strain, Synechococcus sp. WH8103, it could be detected in both the cell wall fraction and the periplasm. The gene (designated pstS) encoding this polypeptide was cloned and shown to be present in a single copy. The deduced amino acid sequence indicated a polypeptide consisting of 326 amino acids with a calculated Mr of 33763. Comparison of this sequence with that obtained by microsequencing the N-terminus of the 32kDa polypeptide showed that the mature protein was synthesized as a precursor, the first 24 amino acid residues being cleaved between two alanine residues at positions 24 and 25. The amino acid sequence of the mature polypeptide showed 35% identity and 52% similarity to the periplasmic phosphate-binding protein (PstS) from Escherichia coli, including three regions of much stronger homology which, by comparison with E. coli PstS, are directly involved in phosphate binding. Northern blot analysis revealed a pstS transcript of 1.2 kb in RNA extracted from cells grown in Pi-replete conditions and one of 1.4 kb in considerably increased abundance under Pi-depleted conditions. Homologues of the pstS gene were detected in other marine phycoerythrin-containing Synechococcus strains, but not in freshwater or halotolerant species.
    Type of Medium: Electronic Resource
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  • 8
    ISSN: 1432-1432
    Keywords: Key words:Prochlorococcus—Synechococcus— Cyanobacteria — Picophytoplankton — Photosynthetic picoplankton — Prochlorophyte — Molecular evolution — Gene clusters
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract. Cultured isolates of the unicellular planktonic cyanobacteria Prochlorococcus and marine Synechococcus belong to a single marine picophytoplankton clade. Within this clade, two deeply branching lineages of Prochlorococcus, two lineages of marine A Synechococcus and one lineage of marine B Synechococcus exhibit closely spaced divergence points with low bootstrap support. This pattern is consistent with a near-simultaneous diversification of marine lineages with divinyl chlorophyll b and phycobilisomes as photosynthetic antennae. Inferences from 16S ribosomal RNA sequences including data for 18 marine picophytoplankton clade members were congruent with results of psbB and petB and D sequence analyses focusing on five strains of Prochlorococcus and one strain of marine A Synechococcus. Third codon position and intergenic region nucleotide frequencies vary widely among members of the marine picophytoplankton group, suggesting that substitution biases differ among the lineages. Nonetheless, standard phylogenetic methods and newer algorithms insensitive to such biases did not recover different branching patterns within the group, and failed to cluster Prochlorococcus with chloroplasts or other chlorophyll b-containing prokaryotes. Prochlorococcus isolated from surface waters of stratified, oligotrophic ocean provinces predominate in a lineage exhibiting low G + C nucleotide frequencies at highly variable positions.
    Type of Medium: Electronic Resource
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  • 9
    ISSN: 1573-5028
    Keywords: Synechococcus ; glucose-6-phosphate dehydrogenase ; cyanobacterium
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The glucose-6-phosphate dehydrogenase (EC 1.1.1.49) gene (zwf) of the cyanobacterium Synechococcus PCC 7942 was cloned on a 2.8 kb Hind III fragment. Sequence analysis revealed an ORF of 1572 nucleotides encoding a polypeptide of 524 amino acids which exhibited 41% identity with the glucose-6-phosphate dehydrogenase of Escherichia coli.
    Type of Medium: Electronic Resource
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  • 10
    ISSN: 1573-5176
    Keywords: Cyanobacteria ; picoplankton ; transcriptional activator ; Synechococcus WH7803 ; phosphate acquisition
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Sequence analysis immediately downstream (3′) of a genomic region ofSynechococcus sp. WH7803, encoding a periplasmic phosphate-binding protein (PstS), revealed an open reading frame encoding a protein of 224 amino acids. The protein exhibited considerable sequence similarity to a family of bacterial transcriptional activators that includes Crp and Fnr and consequently the ORF is designatedptrA (putativetranscriptional activator). Upstream ofptrA a 18 nucleotide sequence representing a putative Pho box was found. Homologues of theptrA gene were detected in several other phycoerythrin-containing marineSynechococcus strains. This represents the third cyanobacterial member of this class of DNA-binding protein to be described and the first such homologue in the ecologically important marineSynechococcus group. The location ofptrA immediately downstream frompstS may implicate this protein in global phosphate regulation.
    Type of Medium: Electronic Resource
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