ArticleGenetics2013
The protein chaperone HSP90 can facilitate the divergence of gene duplicates.
Article in Genetics, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
28 citing papers in PubMed, 59 citations in OpenAlex.
- Whole-genome sequencing reveals a possible molecular basis of sex determination in the dioecious wild yam Dioscorea tokoro.PLoS genetics · 2026Article
- The Hsp90 Molecular Chaperone as a Global Modifier of the Genotype-Phenotype-Fitness Map: An Evolutionary Perspective.Journal of molecular biology · 2024Review
- Pectin modifications promote haustoria development in the parasitic plant Phtheirospermum japonicum.Plant physiology · 2023Article
- GA-Mediated Disruption of RGA/BZR1 Complex Requires HSP90 to Promote Hypocotyl Elongation.International journal of molecular sciences · 2022Article
- Article
- Differential maturation and chaperone dependence of the paralogous protein kinases DYRK1A and DYRK1B.Scientific reports · 2022Article
- Transcription factor BES1 interacts with HSFA1 to promote heat stress resistance of plants.The EMBO journal · 2022Article
- Hsp90 interaction networks in fungi-tools and techniques.FEMS yeast research · 2021Review
- Roles of Brassinosteroids in Mitigating Heat Stress Damage in Cereal Crops.International journal of molecular sciences · 2021Review
- Auxin promotion of seedling growth via ARF5 is dependent on the brassinosteroid-regulated transcription factors BES1 and BEH4.Plant direct · 2019Article
- TTL Proteins Scaffold Brassinosteroid Signaling Components at the Plasma Membrane to Optimize Signal Transduction in Arabidopsis.The Plant cell · 2019Article
- Molecular Chaperones Accelerate the Evolution of Their Protein Clients in Yeast.Genome biology and evolution · 2019Article
- Dynamics of Gene Expression in Single Root Cells ofThe Plant cell · 2019Article
- It's not magic - Hsp90 and its effects on genetic and epigenetic variation.Seminars in cell & developmental biology · 2019Review
- Crosstalk of the Brassinosteroid Signalosome with Phytohormonal and Stress Signaling Components Maintains a Balance between the Processes of Growth and Stress Tolerance.International journal of molecular sciences · 2018Review
- Comprehensive analyses of the BES1 gene family in Brassica napus and examination of their evolutionary pattern in representative species.BMC genomics · 2018Article
- Redundancy, Feedback, and Robustness in theFrontiers in genetics · 2018Article
- Sequence-Based Analysis of Thermal Adaptation and Protein Energy Landscapes in an Invasive Blue Mussel (Mytilus galloprovincialis).Genome biology and evolution · 2017Article
- The heat-shock protein/chaperone network and multiple stress resistance.Plant biotechnology journal · 2017Review
- The Molecular Chaperone DnaK Is a Source of Mutational Robustness.Genome biology and evolution · 2016Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
The heat-shock protein 90 (HSP90) acts as a chaperone by ensuring proper maturation and folding of its client proteins. The HSP90 capacitor hypothesis holds that interactions with HSP90 allow proteins to accumulate mutations while maintaining function. Following this logic, HSP90 clients would be predicted to show relaxed selection compared with nonclients. In this study, we identify a new HSP90 client in the plant steroid hormone pathway: the transcription factor BES1. Its closest paralog, BZR1, is not an HSP90 client. This difference in HSP90 client status in two highly similar proteins enabled a direct test of the capacitor hypothesis. We find that BES1 shows relaxed selection compared to BZR1, hallmarks of neo- and subfunctionalization, and dynamic HSP90 client status across independent evolutionary paths. These results suggested that HSP90's influence on gene evolution may be detectable if we compare gene duplicates because duplicates share most other properties influencing evolutionary rate that might otherwise conceal the chaperone's effect. We test this hypothesis using systematically identified HSP90 clients in yeast and observe a significant trend of HSP90 clients evolving faster than their nonclient paralogs. This trend was not detected when yeast clients and nonclients were compared without considering paralog status. Our data provide evidence that HSP90 influences selection on genes encoding its clients and facilitates divergence between gene duplicates.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.