9
views
0
recommends
+1 Recommend
0 collections
    0
    shares
      • Record: found
      • Abstract: not found
      • Article: not found

      CO2assimilation in the chemocline of Lake Cadagno is dominated by a few types of phototrophic purple sulfur bacteria

      , , , , ,
      FEMS Microbiology Ecology
      Wiley-Blackwell

      Read this article at

      ScienceOpenPublisherPubMed
      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          Lake Cadagno is characterized by a compact chemocline that harbors high concentrations of various phototrophic sulfur bacteria. Four strains representing the numerically most abundant populations in the chemocline were tested in dialysis bags in situ for their ability to fix CO₂. The purple sulfur bacterium Candidatus 'Thiodictyon syntrophicum' strain Cad16(T) had the highest CO₂ assimilation rate in the light of the four strains tested and had a high CO₂ assimilation rate even in the dark. The CO₂ assimilation of the population represented by strain Cad16(T) was estimated to be up to 25% of the total primary production in the chemocline. Pure cultures of strain Cad16(T) exposed to cycles of 12 h of light and 12 h of darkness exhibited the highest CO₂ assimilation during the first 4 h of light. The draft genome sequence of Cad16(T) showed the presence of cbbL and cbbM genes, which encode form I and form II of RuBisCO, respectively. Transcription analyses confirmed that, whereas cbbM remained poorly expressed throughout light and dark exposure, cbbL expression varied during the light-dark cycle and was affected by the available carbon sources. Interestingly, the peaks in cbbL expression did not correlate with the peaks in CO₂ assimilation.

          Related collections

          Most cited references57

          • Record: found
          • Abstract: found
          • Article: not found

          Multiple Rubisco forms in proteobacteria: their functional significance in relation to CO2 acquisition by the CBB cycle.

          Rubisco is the predominant enzymatic mechanism in the biosphere by which autotrophic bacteria, algae, and terrestrial plants fix CO(2) into organic biomass via the Calvin-Benson-Basham reductive pentose phosphate pathway. Rubisco is not a perfect catalyst, suffering from low turnover rates, a low affinity for its CO(2) substrate, and a competitive inhibition by O(2) as an alternative substrate. As a consequence of changing environmental conditions over the past 3.5 billion years, with decreasing CO(2) and increasing O(2) in the atmosphere, Rubisco has evolved into multiple enzymatic forms with a range of kinetic properties, as well as co-evolving with CO(2)-concentrating mechanisms to cope with the different environmental contexts in which it must operate. The most dramatic evidence of this is the occurrence of multiple forms of Rubisco within autotrophic proteobacteria, where Forms II, IC, IBc, IAc, and IAq can be found either singly or in multiple combinations within a particular bacterial genome. Over the past few years there has been increasing availability of genomic sequence data for bacteria and this has allowed us to gain more extensive insights into the functional significance of this diversification. This paper is focused on summarizing what is known about the diversity of Rubisco forms, their kinetic properties, development of bacterial CO(2)-concentrating mechanisms, and correlations with metabolic flexibility and inorganic carbon environments in which proteobacteria perform various types of obligate and facultative chemo- and photoautotrophic CO(2) fixation.
            Bookmark
            • Record: found
            • Abstract: found
            • Article: not found

            A single-cell view on the ecophysiology of anaerobic phototrophic bacteria.

            Quantitative information on the ecophysiology of individual microorganisms is generally limited because it is difficult to assign specific metabolic activities to identified single cells. Here, we develop and apply a method, Halogen In Situ Hybridization-Secondary Ion Mass Spectroscopy (HISH-SIMS), and show that it allows simultaneous phylogenetic identification and quantitation of metabolic activities of single microbial cells in the environment. Using HISH-SIMS, individual cells of the anaerobic, phototropic bacteria Chromatium okenii, Lamprocystis purpurea, and Chlorobium clathratiforme inhabiting the oligotrophic, meromictic Lake Cadagno were analyzed with respect to H(13)CO(3)(-) and (15)NH(4)(+) assimilation. Metabolic rates were found to vary greatly between individual cells of the same species, showing that microbial populations in the environment are heterogeneous, being comprised of physiologically distinct individuals. Furthermore, C. okenii, the least abundant species representing approximately 0.3% of the total cell number, contributed more than 40% of the total uptake of ammonium and 70% of the total uptake of carbon in the system, thereby emphasizing that numerically inconspicuous microbes can play a significant role in the nitrogen and carbon cycles in the environment. By introducing this quantification method for the ecophysiological roles of individual cells, our study opens a variety of possibilities of research in environmental microbiology, especially by increasing the ability to examine the ecophysiological roles of individual cells, including those of less abundant and less active microbes, and by the capacity to track not only nitrogen and carbon but also phosphorus, sulfur, and other biological element flows within microbial communities.
              Bookmark
              • Record: found
              • Abstract: found
              • Article: not found

              Distinct form I, II, III, and IV Rubisco proteins from the three kingdoms of life provide clues about Rubisco evolution and structure/function relationships.

              There are four forms of ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco) found in nature. Forms I, II, and III catalyse the carboxylation and oxygenation of ribulose 1,5-bisphosphate, while form IV, also called the Rubisco-like protein (RLP), does not catalyse either of these reactions. There appear to be six different clades of RLP. Although related to bona fide Rubisco proteins at the primary sequence and tertiary structure levels, RLP from two of these clades is known to perform other functions in the cell. Forms I, II, and III Rubisco, along with form IV (RLP), are thought to have evolved from a primordial archaeal Rubisco. Structure/function studies with both archaeal form III (methanogen) and form I (cyanobacterial) Rubisco have identified residues that appear to be specifically involved with interactions with molecular oxygen. A specific region of all form I, II, and III Rubisco was identified as being important for these interactions.
                Bookmark

                Author and article information

                Journal
                FEMS Microbiology Ecology
                FEMS Microbiol Ecol
                Wiley-Blackwell
                01686496
                May 2013
                May 2013
                : 84
                : 2
                : 421-432
                Article
                10.1111/1574-6941.12074
                23330958
                1fe69a23-44e9-4145-a67f-05f18411878b
                © 2013
                History

                Comments

                Comment on this article