ArticlePloS one2014
Mechanism of deep-sea fish α-actin pressure tolerance investigated by molecular dynamics simulations.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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8 citing papers in PubMed, 22 citations in OpenAlex.
- Pressure-tolerant Evolution in Rhodopsin of Deep-diving Whales.Genome biology and evolution · 2026Article
- High hydrostatic pressure promotes gene transcription via a cystathionine-β-synthase domain-containing protein in the hyperthermophilic archaeon Pyrococcus yayanosii.Nucleic acids research · 2025Article
- Homeocurvature adaptation of phospholipids to pressure in deep-sea invertebrates.Science (New York, N.Y.) · 2024Article
- Distribution of the Order Lampriformes in the Mediterranean Sea with Notes on Their Biology, Morphology, and Taxonomy.Biology · 2022Review
- Convergent Evolution and Structural Adaptation to the Deep Ocean in the Protein-Folding Chaperonin CCTα.Genome biology and evolution · 2020Article
- Session 1SHA-control of biological functions with hydrostatic pressure stimulation.Biophysical reviews · 2020Article
- High pressure inhibits signaling protein binding to the flagellar motor and bacterial chemotaxis through enhanced hydration.Scientific reports · 2020Article
- Molecular adaptation to high pressure in cytochrome P450 1A and aryl hydrocarbon receptor systems of the deep-sea fish Coryphaenoides armatus.Biochimica et biophysica acta. Proteins and proteomics · 2018Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The pressure tolerance of monomeric α-actin proteins from the deep-sea fish Coryphaenoides armatus and C. yaquinae was compared to that of non-deep-sea fish C. acrolepis, carp, and rabbit/human/chicken actins using molecular dynamics simulations at 0.1 and 60 MPa. The amino acid sequences of actins are highly conserved across a variety of species. The actins from C. armatus and C. yaquinae have the specific substitutions Q137K/V54A and Q137K/L67P, respectively, relative to C. acrolepis, and are pressure tolerant to depths of at least 6000 m. At high pressure, we observed significant changes in the salt bridge patterns in deep-sea fish actins, and these changes are expected to stabilize ATP binding and subdomain arrangement. Salt bridges between ATP and K137, formed in deep-sea fish actins, are expected to stabilize ATP binding even at high pressure. At high pressure, deep-sea fish actins also formed a greater total number of salt bridges than non-deep-sea fish actins owing to the formation of inter-helix/strand and inter-subdomain salt bridges. Free energy analysis suggests that deep-sea fish actins are stabilized to a greater degree by the conformational energy decrease associated with pressure effect.
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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.