Intrinsic structural disorder on proteins is involved in the interactome evolution

MARINA UHART; LUIS G. MOYANO; DIEGO MASONE; DIEGO BUSTOS

mendoza

Congreso; A2B2C 10th Meeting; 2019

Asociación Argentina de Bioinformática y Biología Computacional

BACKGROUND: 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 remain 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.RESULTS: Here, we analyzed 9 up-to-date interactomes from the prokaryotic 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 a strict correlation to the contents of protein intrinsic structural disorder. Also, this correlation between these two variables is conserved along with orthologs families in yeast, mouse, and human. About protein function, we found that subcellular localization of the protein, participation on different protein complexes also determine their position in the hyperbolic space.CONCLUSIONS: We conclude that such information is encrypted in the network topology that can be discovered by the new techniques of network embedding.