Cited by 61Protein Structure and DynamicsPhysiological and biochemical adaptationsHemoglobin structure and function

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Structure-based Analysis of High Pressure Adaptation of α-Actin

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Morita, Takami·2003·Journal of Biological Chemistry

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Abstract

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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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)
DOI: 10.1074/jbc.m302328200
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: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 6306 d)
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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Structure-based Analysis of High Pressure Adaptation of α-Actin

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