The DOI matches its Crossref record; 47 of the 47 references it cites were found in a registry or an index.
Structure-based Analysis of High Pressure Adaptation of α-Actin
Open accessAbstract
Deep-sea fishes occur to depths of several thousand meters, and at these abyssal depths encounter pressures that shallower living fishes cannot tolerate. Tolerance of abyssal pressures by deep-sea fish is likely to depend in part on adaptive modifications of proteins. However, the types of structural modifications to proteins that allow function at high pressure have not been discovered. To elucidate the mechanisms of protein adaptation to high pressure, we cloned the alpha-skeletal actin cDNAs from two abyssal Coryphaenoides species, C. armatus and C. yaquinae, and identified three amino acid substitutions, V54A or L67P, Q137K, and A155S, that distinguish these abyssal actins from orthologs of alpha-actin from non-abyssal Coryphaenoides. These substitutions, Q137K and A155S, prevent the dissociation reactions of ATP and Ca2+ from being influenced by high pressure. In particular, the lysine residue at position 137 results in a much smaller apparent volume change in the Ca2+ dissociation reaction. The V54A or L67P substitution reduces the volume change associated with actin polymerization and has a role in maintaining the DNase I activity of actin at high pressure. Together, these results indicate that a few amino acid substitutions in key functional positions can adaptively alter the pressure sensitivity of a protein.
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“Proteins from deep-sea organisms have been found to have structural adaptations that confer some pressure resistance (9, 10).”
From Marine fish may be biochemically constrained from inhabiting the deepest ocean depths (2014) · cites this paper as [10]
In the citing paper
“Hydrostatic pressure can have large inhibitory effects on cellular structures, including proteins.”
From Marine fish may be biochemically constrained from inhabiting the deepest ocean depths (2014) · cites this paper as [10]
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Metadata
- Authors
- Morita, T.
- Corresponding author
- Morita, Takami
- ORCID
- Morita, Takami
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2003-07
- Volume
- 278
- Issue
- 30
- Pages
- 28060-28066
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2077747135
- Cited by
- 58
- References
- 47
- Citations by year
- 2026: 1 · 2025: 2 · 2024: 3 · 2022: 4 · 2021: 5 · 2020: 5 · 2019: 1 · 2018: 2 · 2017: 3 · 2015: 4 · 2014: 4 · 2013: 2
- FWCI
- 0.46
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Physical Sciences › Environmental Science › Ecology › Physiological and biochemical adaptations
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Hemoglobin structure and function
- Keywords
- alpha-actin, high-pressure adaptation, deep-sea fish, Coryphaenoides armatus, amino acid substitutions, calcium dissociation, actin polymerization, skeletal muscle actin
- MeSH terms
- Actins, Adenosine Triphosphate, Animals, Calcium, Cloning, Molecular, Deoxyribonuclease I, Fishes, Lysine, Models, Molecular, Molecular Sequence Data, Phylogeny, Pressure, Species Specificity, Tryptophan, DNA, Complementary, Reverse Transcriptase Polymerase Chain Reaction
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