Background: Bacteria of genus Thermus inhabit both man-made and natural thermal environments. Several Thermus species have shown biotechnological potential such as reduction of heavy metals which is essential for eradication of heavy metal pollution; removing of organic contaminants in water; opening clogged pipes, controlling global warming among many others. Enzymes from thermophilic bacteria have exhibited higher activity and stability than synthetic or enzymes from mesophilic organisms.
Results: Using Meiothermus silvanus DSM 9946 as a reference genome, high level of coordinated rearrangements has been observed in extremely thermophilic Thermus that may imply existence of yet unknown evolutionary forces controlling adaptive re-organization of whole genomes of thermo-extremophiles. However, no remarkable differences were observed across species on distribution of functionally related genes on the chromosome suggesting constraints imposed by metabolic networks. The metabolic network exhibit evolutionary pressures similar to levels of rearrangements as measured by the cross-clustering index. Using stratigraphic analysis of donor-recipient, intensive gene exchanges were observed from Meiothermus species and some unknown sources to Thermus species confirming a well established DNA uptake mechanism as previously proposed.
Conclusion: Global genome rearrangements were found to play an important role in the evolution of Thermus bacteria at both genomic and metabolic network levels. Relatively higher level of rearrangements was observed in extremely thermophilic Thermus strains in comparison to the thermo-tolerant Thermus scotoductus. Rearrangements did not significantly disrupt operons and functionally related genes. Thermus species appeared to have a developed capability for acquiring DNA through horizontal gene transfer as shown by the donor-recipient stratigraphic analysis.
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http://dx.doi.org/10.1186/1471-2164-15-813 | DOI Listing |
Appl Microbiol Biotechnol
January 2025
Department of Biotechnology, Universidad Autónoma Metropolitana-Iztapalapa, Av. Ferrocarril San Rafael Atlixco 186, Col. Leyes de Reforma 1A Sección, Iztapalapa, CDMX, Mexico City, Mexico.
The relationship of microbial community and cometabolic consumption of 2-chlorophenol (2-CP) in a nitrifying sequencing batch reactor (SBR) was studied. The assessment of the population dynamics of the nitrifying sludge during the cometabolic 2-CP consumption with increasing ammonium (NH) concentrations in the SBR showed the presence of 39 different species of which 10 were always present in all cycles. Fifty-five percent of the species found were grouped as Proteobacteria (45% as β-proteobacteria and 10% as γ-proteobacteria class), 30% as Acidobacteria, and 15% as Deinococcus-Thermus phyla.
View Article and Find Full Text PDFFEMS Microbiol Ecol
January 2025
Department of Computer Science, School of Engineering and Natural Sciences, University of Iceland, Dunhagi 5, 107 Reykjavik, Iceland.
The thermophilic bacterium Rhodothermus marinus has mainly been studied for its thermostable enzymes. More recently, the potential of using the species as a cell factory and in biorefinery platforms has been explored, due to the elevated growth temperature, native production of compounds such as carotenoids and exopolysaccharides, the ability to grow on a wide range of carbon sources including polysaccharides, and available genetic tools. A comprehensive understanding of the metabolism of cell factories is important.
View Article and Find Full Text PDFInt J Mol Sci
December 2024
Department of Molecular Biotechnology, Faculty of Chemistry, University of Gdansk, 80-309 Gdansk, Poland.
The increasing antibiotic resistance among bacteria challenges the biotech industry to search for new antibacterial molecules. Endolysin TP84_28 is a thermostable, lytic enzyme, encoded by the bacteriophage (phage) TP-84, and it effectively digests host bacteria cell wall. Biofilms, together with antibiotic resistance, are major problems in clinical medicine and industry.
View Article and Find Full Text PDFInorg Chem
December 2024
Aix Marseille Univ, CNRS, BIP UMR7281, IMM, IM2B, Marseille 13009, France.
Mono-pyranopterin-containing sulfite-oxidizing enzymes (SOEs), including eukaryotic sulfite oxidases and homologous prokaryotic sulfite dehydrogenases (SDHs), are molybdenum enzymes that exist in almost all forms of life, where they catalyze the direct oxidation of sulfite into sulfate, playing a key role in protecting cells and organisms against sulfite-induced damage. To decipher their catalytic mechanism, we have previously provided structural and spectroscopic evidence for direct coordination of HPO to the Mo atom at the active site of the SDH from the hyperthermophilic bacterium (SDH), mimicking the proposed sulfate-bound intermediate proposed to be formed during catalysis. In this work, by solving the X-ray crystallographic structure of the unbound enzyme, we resolve the changes in the hydrogen bonding network in the molybdenum environment that enable the stabilization of the previously characterized phosphate adduct.
View Article and Find Full Text PDFF1000Res
November 2024
Department of Biological Sciences, University of Embu, Embu, Kenya.
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