Protein isoelectric point distribution in the interactomes across the domains of life.

The distribution of the protein isoelectric point (pI) in the protein-protein interaction (PPI) networks across the domains of life has not been investigated yet. This work attempts to correlate the pI with the number of direct interacting partners in the experimentally supported networks involving 226.085 PPIs from 14 various organisms including human, mouse, yeast, bacteria, viruses and 53.606 virus-host interactions. The results showed that the acidic proteins (pI<3) have the highest average number of interactions in eukaryotes, while in bacteria more neutral proteins. On the contrary, the basic proteins (pI>11) have the lowest average number of interactions in human, mouse, yeast, bacteria and human-viral interactomes and the highest average in intraviral interactomes. We examined the correlation of the pI of the interacting partners by calculating the assortativity index of various PPI networks. We found that the interactions between the acidic, neutral and basic proteins have a fairly random mix, implying weak if any association between the acidic and basic proteins. Furthermore, protein features such as biological function, structurally order and disorder, subcellular localization, and homodimerization were classified according to pI in prokaryote and eukaryote proteomes.