A more precise characterization of chaperonin substrates.

Publication Date: 2010 Jun 2 PMID: 20519287
Authors: Raineri, E. – Ribeca, P. – Serrano, L. – Maier, T.
Journal: Bioinformatics

MOTIVATION: Molecular chaperones prevent the aggregation of their substrate proteins and thereby ensure that they reach their functional native state. The bacterial GroEL/ES chaperonin system is understood in great detail on a structural, mechanistic and functional level; its interactors in E.coli have been identified and characterized. However, a long standing question in the field is: What makes a protein a chaperone substrate? RESULTS: Here we identify, using a bioinformatics-based approach a simple set of quantities which characterize the GroEL-substrate proteome. We define three novel parameters differentiating GroEL interactors from other cellular proteins: lower rate of evolution, hydrophobicity and aggregation propensity. Combining them with other known features we manage to identify homologous and heterologous GroEL substrates with good confidence. We discuss our findings in relation to established mechanisms of protein folding and evolutionary buffering by chaperones. CONTACT: tobias.maier@crg.es SUPPLEMENTARY INFORMATION: Supplementary data is available at Bioinformatics online.

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