ArticleBMC evolutionary biology2012
Dissecting the role of low-complexity regions in the evolution of vertebrate proteins.
Article in BMC evolutionary biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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Who cites it
51 citing papers in PubMed, 101 citations in OpenAlex.
- CB-Search: a method for searching for similar protein motifs with biased compositions.BMC bioinformatics · 2026Article
- A benchmarking framework for comparative evaluation of low-complexity region detection tools in the human proteome.Scientific reports · 2026Article
- Low-complexity regions in fungi display functional groups and are depleted in positively charged amino acids.NAR genomics and bioinformatics · 2025Article
- Divergent evolution of low-complexity regions in the vertebrate CPEB protein family.Frontiers in bioinformatics · 2025Article
- LCRAnnotationsDB: a database of low complexity regions functional and structural annotations.BMC genomics · 2024Article
- tRNA regulation and amino acid usage bias reflect a coordinated metabolic adaptation iniScience · 2024Article
- Terminal regions of a protein are a hotspot for low complexity regions and selection.Open biology · 2024Article
- Identification of Low-Complexity Domains by Compositional Signatures Reveals Class-Specific Frequencies and Functions Across the Domains of Life.PLoS computational biology · 2024Article
- Lysine deserts and cullin-RING ligase receptors: Navigating untrodden paths in proteostasis.iScience · 2023Article
- Article
- Low Complexity Regions in Proteins and DNA are Poorly Correlated.Molecular biology and evolution · 2023Article
- Ancient lineages of the keratin-associated protein (KRTAP) genes and their co-option in the evolution of the hair follicle.BMC ecology and evolution · 2023Article
- Protein interactions: anything new?Essays in biochemistry · 2022Article
- Expansion and functional analysis of the SR-related protein family across the domains of life.RNA (New York, N.Y.) · 2022Article
- Insights from analyses of low complexity regions with canonical methods for protein sequence comparison.Briefings in bioinformatics · 2022Article
- Article
- The Repeating, Modular Architecture of the HtrA Proteases.Biomolecules · 2022Article
- Regions with two amino acids in protein sequences: A step forward from homorepeats into the low complexity landscape.Computational and structural biotechnology journal · 2022Article
- Variables Influencing Differences in Sequence Conservation in the Fission Yeast Schizosaccharomyces pombe.Journal of molecular evolution · 2021Article
- The low-complexity domain of the FUS RNA binding protein self-assembles via the mutually exclusive use of two distinct cross-β cores.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundLow-complexity regions (LCRs) in proteins are tracts that are highly enriched in one or a few amino acids. Given their high abundance, and their capacity to expand in relatively short periods of time through replication slippage, they can greatly contribute to increase protein sequence space and generate novel protein functions. However, little is known about the global impact of LCRs on protein evolution.
resultsWe have traced back the evolutionary history of 2,802 LCRs from a large set of homologous protein families from H.sapiens, M.musculus, G.gallus, D.rerio and C.intestinalis. Transcriptional factors and other regulatory functions are overrepresented in proteins containing LCRs. We have found that the gain of novel LCRs is frequently associated with repeat expansion whereas the loss of LCRs is more often due to accumulation of amino acid substitutions as opposed to deletions. This dichotomy results in net protein sequence gain over time. We have detected a significant increase in the rate of accumulation of novel LCRs in the ancestral Amniota and mammalian branches, and a reduction in the chicken branch. Alanine and/or glycine-rich LCRs are overrepresented in recently emerged LCR sets from all branches, suggesting that their expansion is better tolerated than for other LCR types. LCRs enriched in positively charged amino acids show the contrary pattern, indicating an important effect of purifying selection in their maintenance.
conclusionWe have performed the first large-scale study on the evolutionary dynamics of LCRs in protein families. The study has shown that the composition of an LCR is an important determinant of its evolutionary pattern.
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