Contribution by the methanogenic endosymbionts of anaerobic ciliates to methane production in Dutch freshwater sediments

Biogenic methane contributes substantially to the atmospheric methane concentration and thus to global warming. This trace gas is predominantly produced by strictly anaerobic methanogenic archaea, which thrive in the most divergent ecological niches, e. g. paddy fields, sediments, landfills, and the digestive tract of various animals. Methanogenic archaea also live as endosymbionts in the cytoplasm of anaerobic protozoa. In marine sediments these endosymbionts can contribute up to 90% to the overall rate of methanogenesis, whereas their role of in freshwater sediments is largely unknown. Here we describe the results of a one year's survey of the methanogenesis by endosymbiotic methanogens in four different Dutch freshwater sediments. The abundance of anaerobic protozoa, in particular ciliates, the methane production rates by the ecosystem and by the protists, and a number of abiotic parameters were measured. A novel method (heatshock for 5 min) for estimating the contribution by endosymbiotic methanogens was established. Our results reveal large fluctuations of ciliate abundance throughout the year, but on average, only minor contributions by methanogenic endosymbionts to the total methanogenesis in these environment

Cytosolic enzymes with a mitochondrial ancestry from the anaerobic chytrid Piromyces sp. E2

The anaerobic chytrid Piromyces sp. E2 lacks mitochondria, but contains hydrogen-producing organelles, the hydrogenosomes. We are interested in how the adaptation to anaerobiosis influenced enzyme compartmentalization in this organism. Random sequencing of a cDNA library from Piromyces sp. E2 resulted in the isolation of cDNAs encoding malate dehydrogenase, aconitase and acetohydroxyacid reductoisomerase. Phylogenetic analysis of the deduced amino acid sequences revealed that they are closely related to their mitochondrial homologues from aerobic eukaryotes. However, the deduced sequences lack N-terminal extensions, which function as mitochondrial leader sequences in the corresponding mitochondrial enzymes from aerobic eukaryotes. Subcellular fractionation and enzyme assays confirmed that the corresponding enzymes are located in the cytosol. As anaerobic chytrids evolved from aerobic, mitochondria-bearing ancestors, we suggest that, in the course of the adaptation from an aerobic to an anaerobic lifestyle, mitochondrial enzymes were retargeted to the cytosol with the concomitant loss of their N-terminal leader sequences

A hydrogenosome with pyruvate formate-lyase: Anaerobic chytrid fungi use an alternative route for pyruvate catabolism

The chytrid fungi Piromyces sp. E2 and Neocallimastix sp. L2 are obligatory amitochondriate anaerobes that possess hydrogenosomes. Hydrogenosomes are highly specialized organelles engaged in anaerobic carbon metabolism; they generate molecular hydrogen and ATP. Here, we show for the first time that chytrid hydrogenosomes use pyruvate formate-lyase (PFL) and not pyruvate:ferredoxin oxidoreductase (PFO) for pyruvate catabolism, unlike all other hydrogenosomes studied to date. Chytrid PFLs are encoded by a multigene family and are abundantly expressed in Piromyces sp. E2 and Neocallimastix sp. L2. Western blotting after cellular fractionation, proteinase K protection assays and determinations of enzyme activities reveal that PFL is present in the hydrogenosomes of Piromyces sp. E2. The main route of the hydrogenosomal carbon metabolism involves PFL; the formation of equimolar amounts of formate and acetate by isolated hydrogenosomes ex

Effect of dietary changes on the bacteriophage population in the rumen of sheep

Item does not contain fulltext4th Symposium on Gut Microbiology, 21 juni 200

(Endo)symbiotic Methanogenic Archaea

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Anaerobic ciliates and their methanogenic endosymbionts

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Eukaryotic molecular biodiversity: Systematic approaches for the assessment of symbiotic associations

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Clermont Ferrand Workshop Rumen protozoa (invitation). . Acquired knowledge by Ercule and Cimes European programmes

Item does not contain fulltext21 juni 2004Clermont-Ferrand, France : [S.n.