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Extremophile organisms are known that can metabolize at temperatures down to – 25 °C (psychrophiles) and up to 122 °C (hyperthermophiles). Understanding viability under extreme conditions is relevant for human health, biotechnological applications, and our search for life elsewhere in the universe. Information about the stability and dynamics of proteins under environmental extremes is an important factor in this regard. Here we compare the dynamics of small Fe-S proteins – rubredoxins – from psychrophilic and hyperthermophilic microorganisms, using three different nuclear techniques as well as molecular dynamics calculations to quantify motion at the Fe site. The theory of ‘corresponding states’more » posits that homologous proteins from different extremophiles have comparable flexibilities at the optimum growth temperatures of their respective organisms. Although ‘corresponding states’ would predict greater flexibility for rubredoxins that operate at low temperatures, we find that from 4 to 300 K, the dynamics of the Fe sites in these homologous proteins are essentially equivalent.« less

Biofuels are anticipated to enable a shift from fossil fuels for renewable transportation and manufacturing fuels, with biohydrogen considered attractive since it could offer the largest reduction of global carbon budgets. Currently, lignocellulosic biohydrogen production remains inefficient with pretreatments that are heavily fossil fuel-dependent. However, bacteria using alkali-treated biomass could streamline biofuel production while reducing costs and fossil fuel needs. An alkaliphilic bacterium, Halanaerobium hydrogeniformans, is described that is capable of biohydrogen production at levels rivaling neutrophilic strains, but at pH 11 and hypersaline conditions. H. hydrogeniformans ferments a variety of 5- and 6-carbon sugars derived from hemicellulose and cellulosemore » including cellobiose, and forms the end products hydrogen, acetate, and formate. Further, it can also produce biohydrogen from switchgrass and straw pretreated at temperatures far lower than any previously reported and in solutions compatible with growth. Hence, this bacterium can potentially increase the efficiency and efficacy of biohydrogen production from renewable biomass resources.« less

Members of the genus Exiguobacterium are found in diverse environments from marine and fresh waters to permafrost and hot springs. As such, they can grow at a wide range of temperature, pH, salinity, and heavy-metal concentrations. Here we propose Exiguobacterium pavilionensis sp. nov. strain RW2 using phylogenetic, biochemical, and genome analyses. Isolated from a cold freshwater microbialite in Pavilion Lake, British Columbia, E. pavilionensis can grow between 4 and 50 °C, the broadest temperature range reported for the genus. The three Mbp circular genome includes a large set of core genes associated with stress responses to temperature, salinity and heavymore » metals that are conserved among all sequenced strains of Exiguobacterium spp., and which may explain their distribution across such a wide range of ecosystems. We also nominate potential pathways involved in carbonate precipitation (and therefore microbialite formation), as well as carotenoid biosynthesis that could lend the characteristic orange color to members of the genus. The unexpectedly high thermal tolerance of this cold-water bacterium, as well as its latent flagellum synthesis operons, suggest that this species may have had its evolutionary origins in a much warmer environment in which motility was important. These results provide further insight into the potential of Exiguobacterium to exploit a wide range of environmental conditions.« less

Exosialidases are glycoside hydrolases that remove a single terminal sialic acid residue from oligosaccharides. They are widely distributed in biology, having been found in prokaryotes, eukaryotes, and certain viruses. Most characterized prokaryotic sialidases are from organisms that are pathogenic or commensal with mammals. However, in this study, we used functional metagenomic screening to seek microbial sialidases encoded by environmental DNA isolated from an extreme ecological niche, a thermal spring. Using recombinant expression of potential exosialidase candidates and a fluorogenic sialidase substrate, we discovered an exosialidase having no homology to known sialidases. Phylogenetic analysis indicated that this protein is a membermore » of a small family of bacterial proteins of previously unknown function. Proton NMR revealed that this enzyme functions via an inverting catalytic mechanism, a biochemical property that is distinct from those of known exosialidases. This unique inverting exosialidase defines a new CAZy glycoside hydrolase family we have designated GH156« less