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Biology subjects

Gomes, I. S.

Publications and source records attributed to Gomes, I. S..

2 recordsLinked to original sources

A role for HDAC3 in regulating histone lactylation and maintaining oocyte chromatin architecture and fertility

The establishment of specialized chromatin architecture is critical for oocyte development, meiotic fidelity, and embryogenesis. Histone lysine lactylation (Kla) has recently emerged as a widespread chromatin modification, yet its developmental dynamics and function in the germ line remain unclear. Here, we define the temporal profile of Kla during Drosophila oogenesis and identified enzymes that regulate its levels. Kla is absent in early germarial stages, becomes highly enriched during prophase I as meiotic chromosomes condense into the karyosome, and decreases when the karyosome decompacts during transcriptional reactivation. Germline depletion of HDAC3 and Nej/p300 reduces Kla in stage-10 oocytes, revealing conserved chromatin-modifying enzymes that maintain lactylation. Among these, HDAC3 is essential for sustaining karyosome architecture, assembling a normal meiotic spindle, and supporting fertility. These findings identify histone lactylation as a dynamic chromatin feature of oogenesis and suggest that Kla contributes to the establishment of meiotic chromatin states required for oocyte competence. SUMMARY STATEMENTHistone lactylation is developmentally regulated during Drosophila oogenesis. HDAC3 maintains histone lactylation and is essential for meiotic chromatin architecture, meiotic progression, and female fertility.

developmental biology↗

PRIorI: a graph-based mining of structural arrangements in protein-protein interfaces

SummaryProtein-protein interactions (PPIs) are fundamental to biological processes and central to understanding disease mechanisms, making them essential for drug discovery, peptide-based therapeutics, and vaccine development. Identifying conserved structural arrangements within PPI interfaces can provide valuable insights into molecular recognition and interaction mechanisms. Here, we introduce PRIorI (PRotein-PRotein InteractiOn gRaph Isomorphism), a web-based platform to explore precomputed protein-protein interaction networks and identify conserved atomic-level interaction motifs within structural complexes. Unlike traditional methods, PRIorI models PPI interfaces as bipartite graphs, applying graph isomorphism techniques to efficiently retrieve interaction patterns independent of sequence alignment or structural superimposition. Users can query precomputed PDB interaction graphs, upload custom protein structures, or design structural motifs for targeted searches. To illustrate its applicability, we used PRIorI to analyze the SARS-CoV-2 Spike-ACE2 interface, identifying key interaction motifs previously reported in the literature. The platform successfully identified salt bridges, hydrogen bonds, and hydrophobic interactions that stabilize the viral-host complex, demonstrating PRIorIs utility in protein interaction analysis. Availability and implementationWebserver implemented using typescript, python, Next.js and Express.js. Uses MongoDB for storage, Redis for cache and is hosted by Apache on an Ubuntu Server. PRIorI web platform is freely available at https://priori.ufv.br/. Contactsabrina@ufv.br Supplementary informationSupplementary data are available at Bioinformatics online.

bioinformatics↗