ArticlePLoS biology2009
Structural basis for the aminoacid composition of proteins from halophilic archea.
Article in PLoS biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 papers.
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Who cites it
84 citing papers in PubMed.
- Divergent evolution of the PRPS enzymes across the tree of life.bioRxiv : the preprint server for biology · 2026Article
- Histone diversity in the archaeal domain of life.Nature communications · 2026Article
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- Coordinated proteome-scale remodeling underlies polyextremophilic survival in Antarctic cryo-hypersaline brines.Frontiers in microbiology · 2026Article
- Exploring the Catalytic Mechanisms of a Newly Identified Salt-Activated Alginate Lyase fromMarine drugs · 2025Article
- Article
- A Native LH1-RC-HiPIP Supercomplex from an Extremophilic Phototroph.Communications biology · 2025Article
- Improving the production and stability of nanobodies.Protein engineering, design & selection : PEDS · 2025Article
- Archaeal LOV domains from Lake Diamante: first functional characterization of a halo-adapted photoreceptor.Frontiers in microbiology · 2025Article
- How sensitive are protein hydration shells to electrolyte concentration and protein composition?Protein science : a publication of the Protein Society · 2025Article
- HaloClass: Salt-Tolerant Protein Classification with Protein Language Models.The protein journal · 2024Article
- Extremely acidic proteomes and metabolic flexibility in bacteria and highly diversified archaea thriving in geothermal chaotropic brines.Nature ecology & evolution · 2024Article
- Article
- Biosignature Molecules Accumulate and Persist in Evaporitic Brines: Implications for Planetary Exploration.Astrobiology · 2024Article
- Electrostatics introduce a trade-off between mesophilic stability and adaptation in halophilic proteins.Protein science : a publication of the Protein Society · 2024Article
- Emergent ribozyme behaviors in oxychlorine brines indicate a unique niche for molecular evolution on Mars.Nature communications · 2024Article
- Expanded phylogeny of extremely halophilic archaea shows multiple independent adaptations to hypersaline environments.Nature microbiology · 2024Article
- How do bacterial endosymbionts work with so few genes?PLoS biology · 2024Article
- Extremozyme-Based Biosensors for Environmental Pollution Monitoring: Recent Developments.Biosensors · 2024Review
- Genomic basis of environmental adaptation in the widespread poly-extremophilic Exiguobacterium group.The ISME journal · 2024Article
24 more citing papers are in PubMed but not listed here.
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Proteins from halophilic organisms, which live in extreme saline conditions, have evolved to remain folded at very high ionic strengths. The surfaces of halophilic proteins show a biased amino acid composition with a high prevalence of aspartic and glutamic acids, a low frequency of lysine, and a high occurrence of amino acids with a low hydrophobic character. Using extensive mutational studies on the protein surfaces, we show that it is possible to decrease the salt dependence of a typical halophilic protein to the level of a mesophilic form and engineer a protein from a mesophilic organism into an obligate halophilic form. NMR studies demonstrate complete preservation of the three-dimensional structure of extreme mutants and confirm that salt dependency is conferred exclusively by surface residues. In spite of the statistically established fact that most halophilic proteins are strongly acidic, analysis of a very large number of mutants showed that the effect of salt on protein stability is largely independent of the total protein charge. Conversely, we quantitatively demonstrate that halophilicity is directly related to a decrease in the accessible surface area.
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