Publications by authors named "D Flament"

RNA helicases perform essential housekeeping and regulatory functions in all domains of life by binding and unwinding RNA molecules. The Ski2-like proteins are primordial helicases that play an active role in eukaryotic RNA homeostasis pathways, with multiple homologs having specialized functions. The significance of the expansion and diversity of Ski2-like proteins in Archaea, the third domain of life, has not yet been established.

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Unlabelled: The mechanisms underpinning the replication of genomic DNA have recently been challenged in . Indeed, the lack of origin of replication has no deleterious effect on growth, suggesting that replication initiation relies on homologous recombination. Recombination-dependent replication (RDR) appears to be based on the recombinase RadA, which is of absolute requirement when no initiation origins are detected.

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Replication Protein A (RPA) is a heterotrimeric single stranded DNA-binding protein with essential roles in DNA replication, recombination and repair. Little is known about the structure of RPA in Archaea, the third domain of life. By using an integrative structural, biochemical and biophysical approach, we extensively characterize RPA from Pyrococcus abyssi in the presence and absence of DNA.

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Evidence of stable liquid water oceans beneath the ice crust of moons within the Solar System is of great interest for astrobiology. In particular, subglacial oceans may present hydrothermal processes in their abysses, similarly to terrestrial hydrothermal vents. Therefore, terrestrial extremophilic deep life can be considered a model for putative icy moon extraterrestrial life.

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Article Synopsis
  • The proteasome system is responsible for degrading damaged or unneeded proteins, including newly formed peptides, but its interaction with translation machinery in Archaea is not well understood.
  • Researchers studied a small protein called Q9UZY3, now named Pbp11, which was identified using the proteasome-activating nucleotidase (PAN) as bait in experiments.
  • Pbp11 has a unique structure and binds to tRNA, indicating it plays a significant role in connecting the proteasome and translation processes, as it interacts with the proteasome machinery and includes various related proteins in its interaction network.
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