6 research outputs found

    Factors determining the vertical profile of dimethylsulfide in the Sargasso Sea during summer

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    14 pages,11 figuresThe major source of reduced sulfur in the remote marine atmosphere is the biogenic compound dimethylsulfide (DMS), which is ubiquitous in the world’s oceans and released through food web interactions. Relevant fluxes and concentrations of DMS, its phytoplankton-produced precursor, dimethylsulfoniopropionate (DMSP) and related parameters were measured during an intensive Lagrangian field study in two mesoscale eddies in the Sargasso Sea during July–August 2004, a period characterized by high mixed-layer DMS and low chlorophyll—the so-called ‘DMS summer paradox’. We used a 1-D vertically variable DMS production model forced with output from a 1-D vertical mixing model to evaluate the extent to which the simulated vertical structure in DMS and DMSP was consistent with changes expected from field-determined rate measurements of individual processes, such as photolysis, microbial DMS and dissolved DMSP turnover, and air–sea gas exchange. Model numerical experiments and related parametric sensitivity analyses suggested that the vertical structure of the DMS profile in the upper 60 m was determined mainly by the interplay of the two depth variable processes—vertical mixing and photolysis—and less by biological consumption of DMS. A key finding from the model calibration was the need to increase the DMS(P) algal exudation rate constant, which includes the effects of cell rupture due to grazing and cell lysis, to significantly higher values than previously used in other regions. This was consistent with the small algal cell size and therefore high surface area-to-volume ratio of the dominant DMSP-producing group—the picoeukaryotes.We gratefully acknowledge the financial assistance provided through NSF Biocomplexity funding (OPP-0083078) and an Australian Research Council Discovery Grant. We are grateful to the comments by D.J. Kieber. We recognize the participation and help of K. Bailey, J. Bisgrove, B. Blomquist, I. Forn, H. Harada, B. Huebert, D. Jones, L. Maroney, A. Neely, S. Riseman, C. Smith, J. Stefels, K. Tinklepaugh, M. Vila-Costa, G. Westby, H. Zemmelink and the R/V Seward Johnson crew. DiTullio et al., 2001; Simo ́ and Dachs, 2002; Simon and Azam, 1989; Zemmelink et al., 2005Peer reviewe

    Exploring early steps in biofilm formation: set-up of an experimental system for molecular studies

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    Background: Bacterial biofilms are predominant in natural ecosystems and constitute a public health threat because of their outstanding resistance to antibacterial treatments and especially to antibiotics. To date, several systems have been developed to grow bacterial biofilms in order to study their phenotypes and the physiology of sessile cells. Although relevant, such systems permit analysis of various aspects of the biofilm state but often after several hours of bacterial growth.Results: Here we describe a simple and easy-to-use system for growing P. aeruginosa biofilm based on the medium adsorption onto glass wool fibers. This approach which promotes bacterial contact onto the support, makes it possible to obtain in a few minutes a large population of sessile bacteria. Using this growth system, we demonstrated the feasibility of exploring the early stages of biofilm formation by separating by electrophoresis proteins extracted directly from immobilized cells. Moreover, the involvement of protein synthesis in P. aeruginosa attachment is demonstrated.Conclusions: Our system provides sufficient sessile biomass to perform biochemical and proteomic analyses from the early incubation period, thus paving the way for the molecular analysis of the early stages of colonization that were inaccessible to date

    Distinct Roles for Key Karyogamy Proteins during Yeast Nuclear Fusion

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    During yeast mating, cell fusion is followed by the congression and fusion of the two nuclei. Proteins required for nuclear fusion are found at the surface (Prm3p) and within the lumen (Kar2p, Kar5p, and Kar8p) of the nuclear envelope (NE). Electron tomography (ET) of zygotes revealed that mutations in these proteins block nuclear fusion with different morphologies, suggesting that they act in different steps of fusion. Specifically, prm3 zygotes were blocked before formation of membrane bridges, whereas kar2, kar5, and kar8 zygotes frequently contained them. Membrane bridges were significantly larger and occurred more frequently in kar2 and kar8, than in kar5 mutant zygotes. The kinetics of NE fusion in prm3, kar5, and kar8 mutants, measured by live-cell fluorescence microscopy, were well correlated with the size and frequency of bridges observed by ET. However the kar2 mutant was defective for transfer of NE lumenal GFP, but not diffusion within the lumen, suggesting that transfer was blocked at the NE fusion junction. These observations suggest that Prm3p acts before initiation of outer NE fusion, Kar5p may help dilation of the initial fusion pore, and Kar2p and Kar8p act after outer NE fusion, during inner NE fusion

    IASIL Bibliography 2013

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