ArticleThe Journal of biological chemistry2013
An extremely halophilic proteobacterium combines a highly acidic proteome with a low cytoplasmic potassium content.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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43 citing papers in PubMed, 80 citations in OpenAlex.
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- A Native LH1-RC-HiPIP Supercomplex from an Extremophilic Phototroph.Communications biology · 2025Article
- Salinity-driven niche differentiation within the aquatic Luna-1 subcluster.ISME communications · 2025Article
- How sensitive are protein hydration shells to electrolyte concentration and protein composition?Protein science : a publication of the Protein Society · 2025Article
- Electrostatics introduce a trade-off between mesophilic stability and adaptation in halophilic proteins.Protein science : a publication of the Protein Society · 2024Article
- The polyextremophileApplied and environmental microbiology · 2024Article
- Living in trinity of extremes: Genomic and proteomic signatures of halophilic, thermophilic, and pH adaptation.Current research in structural biology · 2024Article
- Prevalence and mechanism of synergistic carboxylate-cation-water interactions in halophilic proteins.Biophysical journal · 2023Article
- Extreme fluctuations in ambient salinity select for bacteria with a hybrid "salt-in"/"salt-out" osmoregulation strategy.Frontiers in microbiomes · 2023Article
- Alternative CUG Codon Usage in the Halotolerant YeastJournal of fungi (Basel, Switzerland) · 2022Article
- The Osmoprotectant Switch of Potassium to Compatible Solutes in an Extremely Halophilic ArchaeaGenes · 2022Article
- Salt- and pH-Dependent Thermal Stability of Photocomplexes from Extremophilic BacteriochlorophyllMicroorganisms · 2022Article
- Adaptation to Varying Salinity inFrontiers in microbiology · 2022Article
- Net Charges of the Ribosomal Proteins of theMicrobiology spectrum · 2021Article
- Article
- Proteins maintain hydration at high [KCl] concentration regardless of content in acidic amino acids.Biophysical journal · 2021Article
- A potassium chloride to glycine betaine osmoprotectant switch in the extreme halophile Halorhodospira halophila.Scientific reports · 2020Article
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Halophilic archaea accumulate molar concentrations of KCl in their cytoplasm as an osmoprotectant and have evolved highly acidic proteomes that function only at high salinity. We examined osmoprotection in the photosynthetic Proteobacteria Halorhodospira halophila and Halorhodospira halochloris. Genome sequencing and isoelectric focusing gel electrophoresis showed that the proteome of H. halophila is acidic. In line with this finding, H. halophila accumulated molar concentrations of KCl when grown in high salt medium as detected by x-ray microanalysis and plasma emission spectrometry. This result extends the taxonomic range of organisms using KCl as a main osmoprotectant to the Proteobacteria. The closely related organism H. halochloris does not exhibit an acidic proteome, matching its inability to accumulate K(+). This observation indicates recent evolutionary changes in the osmoprotection strategy of these organisms. Upon growth of H. halophila in low salt medium, its cytoplasmic K(+) content matches that of Escherichia coli, revealing an acidic proteome that can function in the absence of high cytoplasmic salt concentrations. These findings necessitate a reassessment of two central aspects of theories for understanding extreme halophiles. First, we conclude that proteome acidity is not driven by stabilizing interactions between K(+) ions and acidic side chains but by the need for maintaining sufficient solvation and hydration of the protein surface at high salinity through strongly hydrated carboxylates. Second, we propose that obligate protein halophilicity is a non-adaptive property resulting from genetic drift in which constructive neutral evolution progressively incorporates weakly stabilizing K(+)-binding sites on an increasingly acidic protein surface.
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