AI Article Synopsis
- Molecular chaperones, like the GroEL/ES system in bacteria, help proteins fold correctly and prevent them from aggregating, but the specific characteristics that make a protein a substrate for these chaperones have not been fully understood.
- A bioinformatics approach was used to identify key traits of GroEL substrate proteins, distinguishing them from other proteins with factors like lower evolutionary rates, higher hydrophobicity, and greater aggregation potential.
- These findings contribute to our understanding of protein folding processes and the role of chaperones in evolutionary stability.
Article Abstract
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 Escherichia 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 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.
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| http://dx.doi.org/10.1093/bioinformatics/btq287 | DOI Listing |
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