Chaperone client proteins evolve slower than non-client proteins
- PMID: 32377887
- DOI: 10.1007/s10142-020-00740-1
Chaperone client proteins evolve slower than non-client proteins
Abstract
Chaperones are important molecular machinery that assists proteins to attain their native three-dimensional structure crucial for function. Earlier studies using experimental evolution showed that chaperones impose a relaxation of sequence constraints on their "client" proteins, which may lead to the fixation of slightly deleterious mutations on the latter. However, we hypothesized that such a phenomenon might be harmful to the organism in a natural physiological condition. In this study, we investigated the evolutionary rates of chaperone client and non-client proteins in five model organisms from both prokaryotic and eukaryotic lineages. Our study reveals a slower evolutionary rate of chaperone client proteins in all five organisms. Additionally, the slower folding rate and lower aggregation propensity of chaperone client proteins reveal that the chaperone may play an essential role in rescuing the slightly disadvantageous effects due to random mutations and subsequent protein misfolding. However, the fixation of such mutations is less likely to be selected in the natural population.
Keywords: Chaperone; Chaperone client proteins; Evolutionary rate; Protein aggregation propensity; Protein folding rate.
Similar articles
-
Heterogeneous binding of the SH3 client protein to the DnaK molecular chaperone.Proc Natl Acad Sci U S A. 2015 Aug 4;112(31):E4206-15. doi: 10.1073/pnas.1505173112. Epub 2015 Jul 20. Proc Natl Acad Sci U S A. 2015. PMID: 26195753 Free PMC article.
-
Molecular Chaperones Accelerate the Evolution of Their Protein Clients in Yeast.Genome Biol Evol. 2019 Aug 1;11(8):2360-2375. doi: 10.1093/gbe/evz147. Genome Biol Evol. 2019. PMID: 31297528 Free PMC article.
-
Frustrated Interfaces Facilitate Dynamic Interactions between Native Client Proteins and Holdase Chaperones.Chembiochem. 2019 Nov 18;20(22):2803-2806. doi: 10.1002/cbic.201900215. Epub 2019 Sep 17. Chembiochem. 2019. PMID: 31063619
-
Protein folding sculpting evolutionary change.Cold Spring Harb Symp Quant Biol. 2009;74:103-8. doi: 10.1101/sqb.2009.74.043. Epub 2010 Apr 7. Cold Spring Harb Symp Quant Biol. 2009. PMID: 20375316 Review.
-
Molecular chaperones HscA/Ssq1 and HscB/Jac1 and their roles in iron-sulfur protein maturation.Crit Rev Biochem Mol Biol. 2007 Mar-Apr;42(2):95-111. doi: 10.1080/10409230701322298. Crit Rev Biochem Mol Biol. 2007. PMID: 17453917 Review.
Cited by
-
Protein folding in vitro and in the cell: From a solitary journey to a team effort.Biophys Chem. 2022 Aug;287:106821. doi: 10.1016/j.bpc.2022.106821. Epub 2022 Apr 29. Biophys Chem. 2022. PMID: 35667131 Free PMC article. Review.
-
Comparative Study of Protein Aggregation Propensity and Mutation Tolerance Between Naked Mole-Rat and Mouse.Genome Biol Evol. 2022 May 3;14(5):evac057. doi: 10.1093/gbe/evac057. Genome Biol Evol. 2022. PMID: 35482036 Free PMC article.
-
Targeting DNA topoisomerases or checkpoint kinases results in an overload of chaperone systems, triggering aggregation of a metastable subproteome.Elife. 2022 Feb 24;11:e70726. doi: 10.7554/eLife.70726. Elife. 2022. PMID: 35200138 Free PMC article.
