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Archaea represents the third domain of life, displaying a closer relationship with eukaryotes than bacteria. These microorganisms are valuable model systems for molecular biology and biotechnology. In fact, nowadays, methanogens, halophiles, thermophilic euryarchaeota, and crenarchaeota are the four groups of archaea for which genetic systems have been well established, making them suitable as model systems and allowing for the increasing study of archaeal genes' functions. Furthermore, thermophiles are used to explore several aspects of archaeal biology, such as stress responses, DNA replication and repair, transcription, translation and its regulation mechanisms, CRISPR systems, and carbon and energy metabolism. Extremophilic archaea also represent a valuable source of new biomolecules for biological and biotechnological applications, and there is growing interest in the development of engineered strains. In this review, we report on some of the most important aspects of the use of archaea as a model system for genetic evolution, the development of genetic tools, and their application for the elucidation of the basal molecular mechanisms in this domain of life. Furthermore, an overview on the discovery of new enzymes of biotechnological interest from archaea thriving in extreme environments is reported.
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http://dx.doi.org/10.3390/biom13010114 | DOI Listing |
mSphere
September 2025
Department of Biology, Johns Hopkins University, Baltimore, Maryland, USA.
Oxidative stress induces a wide range of cellular damage, often causing disease and cell death. While many organisms are susceptible to the effects of oxidative stress, haloarchaea have adapted to be highly resistant. Several aspects of the haloarchaeal oxidative stress response have been characterized; however, little is known about the impacts of oxidative stress at the translation level.
View Article and Find Full Text PDFBiochem Biophys Res Commun
September 2025
Beamline Development and Application Section, Bhabha Atomic Research Centre, Mumbai, 400085, India. Electronic address:
The UPF0235 UniProt family proteins are conserved across archaea, bacteria, and eukaryotes; however, they remain functionally uncharacterized. Here, we report the high resolution (1.3 Å) crystal structure of UPF0235 protein (PF1765, UniProt: Q8U052) from Pyrococcus furiosus.
View Article and Find Full Text PDFJ Biol Chem
September 2025
Department of Biochemistry and Molecular Biology, Penn State University, University Park, PA, 16802; Center for Structural Biology, Penn State University, University Park, PA 16802; Center for RNA Molecular Biology, Penn State University, University Park, PA 16802. Electronic address:
Despite the overall conservation of ribosomes across all domains of life, differences in their 3D architecture, rRNA sequences, ribosomal protein composition, and translation factor requirements reflect lineage-specific adaptations to environmental niches. In the domain Archaea, structural studies have primarily focused on non-methanogenic thermophiles and halophiles, leaving it unclear whether these represent the broader archaeal domain. Here, we report the cryo-electron microscopy (cryo-EM) structure of the ribosome from Methanosarcina acetivorans, a previously unreported high-resolution structure from a model mesophilic methanogenic archaeon.
View Article and Find Full Text PDFAnaerobic methanotrophic archaea (ANME) are crucial to planetary carbon cycling. They oxidise methane in anoxic niches by transferring electrons to nitrate, metal oxides, or sulfate-reducing bacteria. No ANMEs have been isolated, hampering the biochemical investigation of anaerobic methane oxidation.
View Article and Find Full Text PDFMicrobiol Resour Announc
September 2025
Department of Biology, Portland State University, Portland, Oregon, USA.
Here, we report the circularized complete genome of DSM 3773 (1,856,505 bp, G + C 40.7%). This genome contains 1,955 protein-coding regions and 46 tRNAs.
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