Journal: International Journal of Molecular Sciences
Article Title: Integrated Symbiotic Pleiotropy: Long Non-Coding RNAs and Disordered Proteins Interweaving the Functional Layers of the Eukaryotic Cell
doi: 10.3390/ijms27083478
Figure Lengend Snippet: Biophysical landscapes of Arc orthologs and Gag-related proteins. (Top) 3D structures (PDB), residue-based droplet-promoting probabilities (p DP ), predicted regions of disorder, aggregation, and context-dependent binding (FuzDrop/FuzPred), and UniProt domains/features aligned with the p DP graph of ( A ) D. melanogaster (dArc2) and ( B ) H. sapiens (Arc), illustrating the evolutionary transition from rigid invertebrate architecture to high-disorder and LLPS propensity mammalian condensates. (Bottom) ( C ) Comparative analysis of p LLPS propensity, protein disorder, and amyloidogenic potential across 30+ species. Left Y-axis: p LLPS and disorder scores (0.0–1.0). Right Y-axis: Number of amyloidogenic segments (PASTA 2.0). Yellow/Pink bars: Evolutionary benchmarks (HIV-1 Gag, PERV Gag, and PEG10) revealing the high ancestral propensity for phase separation and aggregation. Light-blue bars: Drosophila convergent homologs (dArc1, dArc2); dark-blue bars: vertebrate orthologs, highlighting the significant “mammalian shift” in p LLPS . Red dots: Amyloidogenic potential, showing discrete “quantal” plateaus (7–8 for Sauropsids vs. 38 for Eutherians). Stars: Red and blue stars denote significant outliers in amyloidogenic potential (notably the Indian elephant) and p LLPS propensity, respectively. Note: The proposed evolutionary trajectories and “quantum leaps” of these biophysical parameters are discussed in detail within the main text .
Article Snippet: Taxon-dependent clustering: Our results show clear phylogenetic clustering of p LLPS values ( C).
Techniques: Residue, Binding Assay