Publications by authors named "Giada Finocchio"
Article Synopsis
- Argonaute proteins play essential roles in RNA silencing, helping regulate gene expression and defend against viruses and transposons in eukaryotes, with two main types: AGOs for miRNA/siRNA and PIWIs for piRNA.
- Research shows that a specific Argonaute protein, HrAgo1, from the Lokiarchaeon 'Candidatus Harpocratesius repetitus,' shares a common ancestry with eukaryotic PIWI proteins and is capable of RNA-guided RNA cleavage.
- The study suggests that HrAgo1 retains ancient structural features, hinting at how Argonaute proteins might have evolved and diverged in the early stages of eukaryotic development.
In both prokaryotic and eukaryotic innate immune systems, TIR domains function as NADases that degrade the key metabolite NAD+ or generate signaling molecules. Catalytic activation of TIR domains requires oligomerization, but how this is achieved varies in distinct immune systems. In the Short prokaryotic Argonaute (pAgo)/TIR-APAZ (SPARTA) immune system, TIR NADase activity is triggered upon guide RNA-mediated recognition of invading DNA by an unknown mechanism.
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- Proton-dependent oligopeptide transporters (POTs) play a key role in absorbing various dietary peptides and drugs, but understanding how they transport these different substrates has been a challenge.
- Researchers presented 14 X-ray structures of the bacterial POT DtpB with diverse di- and tripeptides, revealing important information about the transporter's flexible binding site.
- By studying binding affinities of over 80 peptides and using advanced techniques like molecular docking and machine learning, they found that peptides with compact hydrophobic residues are most effectively recognized by DtpB.
Proton-coupled Oligopeptide Transporters (POTs) of the Major Facilitator Superfamily (MFS) mediate the uptake of short di- and tripeptides in all phyla of life. POTs are thought to constitute the most promiscuous class of MFS transporters, with the potential to transport more than 8400 unique substrates. Over the past two decades, transport assays and biophysical studies have shown that various orthologues and paralogues display differences in substrate selectivity.
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