Journal of Proteomics & Bioinformatics

Journal of Proteomics & Bioinformatics
Open Access

ISSN: 0974-276X

+44 1223 790975

Protein complex forming ability is favored over the features of interacting partners in determining the evolutionary rates of proteins in the yeast protein-protein interaction networks


International Conference & Exhibition on Proteomics & Bioinformatics

2011

Sandip Chakraborty, Bratati Kahali and Tapash Chandra Ghosh

Scientific Tracks Abstracts: J Proteomics Bioinform

Abstract :

Evolutionary rates (ERs) of proteins in a protein-protein interaction (PPI) network are primarily governed by the protein connectivity and/or expression level. A recent study revealed the importance of the coefficient of functionality and clustering coefficient in controlling the protein ERs in the PPI network. By multivariate regression analysis we found that the three parameters: probability of complex formation, expression level and connectivity of a protein independently guide the evolutionary rates of proteins in the PPI network. We also found that for complex forming proteins in the network, those which have partners sharing the same functional classes evolve faster than those having partners belonging to different functional classes. The proteins in the dense parts of the network evolve faster than their sparse parts counterparts. Taking into account the complex forming ability, we found that all the complex forming proteins considered in this study evolve slower than the non-complex forming proteins irrespective of their localization in the network or the affiliation of their partners to same/different functional classes. We have shown here that the coefficient of functionality and clustering coefficient is correlated with the protein connectivity in the PPI network. We have identified the significant relationship between the complex-forming property of proteins and their ERs even when they are classified according to the features of their interacting partners. Our study implies that the evolutionarily constrained proteins are actually members of a larger number of protein complexes and this justifies why they have enhanced expression levels.

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