Intrinsic structural disorder on proteins is involved in the interactome evolution

MOYANO, L. G. ; UHART, M.; BUSTOS, D. M.; MASONE, D. F.

Mendoza

Congreso; X Congreso Argentino de Bioinformática y Biología Computacional (10CA2BC); 2019

A2B2C

It has become evident that the generation of big amount of biological data through new sequencing technologies alone are not enough to truly understand cell complexity. Despite having identified the function of hundreds of genes many details of how exactly they contribute to cell physiology obscure. Understanding how cellular systems evolve on a genome-scale is central in biology and medicine. The representation of protein interaction networks in the two-dimensional hyperbolic plane has been shown to be both significant and useful: node coordinates has encrypted information about protein evolution, structure, and function. Here, we analyzed 9 up-to-date interactomes from the prokariotic bacteria E. coli to human. We found that not all the interactomes are strictly scale-free, this deviation appears to be correlative to the completeness of the interactome because model organisms (where the interactomes are more complete) has more low-degree nodes than predicted by the theory. Another interesting finding was that in the 9 cases studied, the hyperbolic coordinate has an strictly correlation to thecontents of protein intrinsic structural disorder. Also, this correlation between these two variables is conserved along orthologs families in yeast, mouse and human. About protein function, we found that subcellular localization of protein, participation on different protein complexes also determine their position in the hyperbolic space. We conclude that much information are encryted in network topologythat can be discover by the new techniques of network embedding.