Send to

Choose Destination
Bioinformatics. 2010 Jul 15;26(14):1685-9. doi: 10.1093/bioinformatics/btq287. Epub 2010 Jun 2.

A more precise characterization of chaperonin substrates.

Author information

CNAG Centro Nacional de AnĂ¡lisis GenĂ³mico, Parc Cientific de Barcelona, Baldiri Reixac 4, E-08028 Barcelona, Spain.



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 Escherichia coli have been identified and characterized. However, a long-standing question in the field is: What makes a protein a chaperone substrate?


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 to a simple Bayesian predictor allows us to identify known homologous and heterologous GroEL substrateproteins. We discuss our findings in relation to established mechanisms of protein folding and evolutionary buffering by chaperones.

[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for Silverchair Information Systems
Loading ...
Support Center