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Biology subjects

Ausiello, G.

Publications and source records attributed to Ausiello, G..

3 recordsLinked to original sources

Cross-Attention Over RNA And Protein Sequences Enables Generalizable Interaction Prediction

Computational predictions are essential to characterize the RNA-protein interaction landscape, yet a persistent gap between benchmark performance and practical utility suggests that current models have limited generalization capabilities. To address this issue, we present CORAL (Cross-attention for RNA-protein Association Learning), a deep learning framework for the prediction of RNA-protein interactions that integrates pretrained protein (ESM-2) and RNA (DNABERT2) language models through bidirectional cross-attention with Low-Rank Adaptation fine-tuning. We also introduce a benchmarking framework that rigorously addresses the problem of data redundancy between training and test sets, which greatly inflates model performances reported in the literature. To this end we adopt three partitioning strategies of increasing stringency: conventional random splits, pairwise non-redundant splits, and component-wise non-redundant splits. CORAL maintains an F1 score of 0.65 under the most stringent component-wise evaluation, compared to 0.47 for the next-best method retaining discriminative behavior. Interpretability analyses further reveal that the cross-attention mechanism captures biologically meaningful features of molecular recognition at two complementary structural scales: at atomic resolution, specific attention heads systematically attend to structurally defined contact positions, showing 26% elevated attention at interface residues across 309 experimentally resolved complexes (p < 0.001); at the domain level, protein-side attention localizes to annotated RNA-binding domains across 94 % of 462 proteins examined (median within-protein Cohens d {approx} 0.94). Together, these findings establish that current RPI prediction benchmarks substantially inflate performance estimates and demonstrate that cross-modal attention architectures yield improved generalization alongside mechanistically interpretable representations.

bioinformatics↗

Human lncRNAs harbor conserved modules embedded in different sequence contexts

We analyzed the structure of human long non-coding RNA (lncRNAs) genes to investigate whether the non-coding transcriptome is organized in modular domains, as is the case for protein-coding genes. To this aim, we compared all known human lncRNA exons and identified 340 pairs of exons with high sequence and/or secondary structure similarity but embedded in a dissimilar sequence context. We grouped these pairs in 106 clusters based on their reciprocal similarities. These shared modules are highly conserved between humans and the four great ape species, display evidence of purifying selection and likely arose as a result of recent segmental duplications. Our analysis contributes to the understanding of the mechanisms driving the evolution of the non-coding genome and suggests additional strategies towards deciphering the functional complexity of this class of molecules. Author summaryThe Human genome includes more than 18,000 genes coding for RNAs that are not translated into proteins, called long non-coding RNAs (lncRNA). Mounting evolutionary and experimental evidence shows that a large amount of these RNAs have a specific function, mainly as regulators of a diverse set of biological processes. Here we set out to investigate whether these genes have a modular organization similar to that of protein-coding genes. Accordingly, we compared the sequence of all the exonic regions of human lncRNAs and identified 106 clusters of non-repetitive exonic modules shared between this class of genes. These modules display evidence of purifying selection, are highly conserved between humans and the four great ape species, and may represent distinct functional units that have been shuffled among multiple lncRNA genes, in a manner similar to the exon-shuffling process that is observed in the coding genome.

evolutionary biology↗

Revisiting the \"satisfaction of spatial restraints\" approach of MODELLER for protein homology modeling

The most frequently used approach for protein structure prediction is currently homology modeling. The 3D model building phase of this methodology is critical for obtaining an accurate and biologically useful prediction. The most widely employed tool to perform this task is MODELLER. This program implements the \"modeling by satisfaction of spatial restraints\" strategy and its core algorithm has not been altered significantly since the early 1990s. In this work, we have explored the idea of modifying MODELLER with two effective, yet computationally light strategies to improve its 3D modeling performance. Firstly, we have investigated how the level of accuracy in the estimation of structural variability between a target protein and its templates in the form of{sigma} values profoundly influences 3D modeling. We show that the{sigma} values produced by MODELLER are on average weakly correlated to the true level of structural divergence between target-template pairs and that increasing this correlation greatly improves the programs predictions, especially in multiple-template modeling. Secondly, we have inquired into how the incorporation of statistical potential terms (such as the DOPE potential) in the MODELLERs objective function impacts positively 3D modeling quality by providing a small but consistent improvement in metrics such as GDT-HA and lDDT and a large increase in stereochemical quality. Python modules to harness this second strategy are freely available at https://github.com/pymodproject/altmod. In summary, we show that there is a large room for improving MODELLER in terms of 3D modeling quality and we propose strategies that could be pursued in order to further increase its performance.\n\nAuthor summaryProteins are fundamental biological molecules that carry out countless activities in living beings. Since the function of proteins is dictated by their three-dimensional atomic structures, acquiring structural details of proteins provides deep insights into their function. Currently, the most successful computational approach for protein structure prediction is template-based modeling. In this approach, a target protein is modeled using the experimentally-derived structural information of a template protein assumed to have a similar structure to the target. MODELLER is the most frequently used program for template-based 3D model building. Despite its success, its predictions are not always accurate enough to be useful in Biomedical Research. Here, we show that it is possible to greatly increase the performance of MODELLER by modifying two aspects of its algorithm. First, we demonstrate that providing the program with accurate estimations of local target-template structural divergence greatly increases the quality of its predictions. Additionally, we show that modifying MODELLERs scoring function with statistical potential energetic terms also helps to improve modeling quality. This work will be useful in future research, since it reports practical strategies to improve the performance of this core tool in Structural Bioinformatics.

bioinformatics↗