Correlation between protein abundance and sequence conservation: what do recent experiments say?
- PMID: 36162152
- DOI: 10.1016/j.gde.2022.101984
Correlation between protein abundance and sequence conservation: what do recent experiments say?
Abstract
Cells evolve in a space of parameter values set by physical and chemical forces. These constraints create associations among cellular properties. A particularly strong association is the negative correlation between the rate of evolution of proteins and their abundance in the cell. Highly expressed proteins evolve slower than lowly expressed ones. Multiple hypotheses have been put forward to explain this relationship, including, for instance, the requirement for higher mRNA stability, misfolding avoidance, and misinteraction avoidance for highly expressed proteins. Here, we review some of these hypotheses, their predictions, and how they are supported to finally discuss recent experiments that have been performed to test these predictions.
Copyright © 2022 Elsevier Ltd. All rights reserved.
Similar articles
-
Protein misinteraction avoidance causes highly expressed proteins to evolve slowly.Proc Natl Acad Sci U S A. 2012 Apr 3;109(14):E831-40. doi: 10.1073/pnas.1117408109. Epub 2012 Mar 13. Proc Natl Acad Sci U S A. 2012. PMID: 22416125 Free PMC article.
-
Protein Stability and Avoidance of Toxic Misfolding Do Not Explain the Sequence Constraints of Highly Expressed Proteins.Mol Biol Evol. 2018 Mar 1;35(3):700-703. doi: 10.1093/molbev/msx323. Mol Biol Evol. 2018. PMID: 29309671
-
N-glycoproteins exhibit a positive expression level-evolutionary rate correlation.J Evol Biol. 2019 Apr;32(4):390-394. doi: 10.1111/jeb.13420. Epub 2019 Mar 5. J Evol Biol. 2019. PMID: 30697857
-
Biophysical Models of Protein Evolution: Understanding the Patterns of Evolutionary Sequence Divergence.Annu Rev Biophys. 2017 May 22;46:85-103. doi: 10.1146/annurev-biophys-070816-033819. Epub 2017 Mar 15. Annu Rev Biophys. 2017. PMID: 28301766 Free PMC article. Review.
-
Why proteins evolve at different rates: the functional hypothesis versus the mistranslation-induced protein misfolding hypothesis.FEBS Lett. 2009 Apr 2;583(7):1053-9. doi: 10.1016/j.febslet.2009.02.033. Epub 2009 Feb 28. FEBS Lett. 2009. Retraction in: FEBS Lett. 2009 Sep 17;583(18):3108. doi: 10.1016/j.febslet.2009.08.024. PMID: 19254718 Retracted. Review.
Cited by
-
The role of metabolism in shaping enzyme structures over 400 million years.Nature. 2025 Aug;644(8075):280-289. doi: 10.1038/s41586-025-09205-6. Epub 2025 Jul 9. Nature. 2025. PMID: 40634610 Free PMC article.
-
Aminoacyl-tRNA Synthetase Evolution within the Dynamic Tripartite Translation System of Plant Cells.Genome Biol Evol. 2023 Apr 6;15(4):evad050. doi: 10.1093/gbe/evad050. Genome Biol Evol. 2023. PMID: 36951086 Free PMC article.
-
Faster adaptation but slower divergence of X chromosomes under paternal genome elimination.Nat Commun. 2025 Jun 11;16(1):5288. doi: 10.1038/s41467-025-60114-8. Nat Commun. 2025. PMID: 40500283 Free PMC article.
-
Community- and genome-based evidence for a shaping influence of redox potential on bacterial protein evolution.mSystems. 2023 Jun 29;8(3):e0001423. doi: 10.1128/msystems.00014-23. Epub 2023 Jun 8. mSystems. 2023. PMID: 37289197 Free PMC article.
-
Epistasis between promoter activity and coding mutations shapes gene evolvability.Sci Adv. 2023 Feb 3;9(5):eadd9109. doi: 10.1126/sciadv.add9109. Epub 2023 Feb 3. Sci Adv. 2023. PMID: 36735790 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources