User:Danielk1m1005/Deep sea
Ideas for the addition to the article[edit]
Most of the edits would go into the Pressure section of the article Deep sea or into the Characteristics section of the article Deep sea fish.
Adaptation to the Pressure in the Deep Sea[edit]
Deep sea fish have different adaptations in their proteins, anatomical structures, and metabolic systems to survive in the Deep sea, where the inhabitants have to withstand great amount of hydrostatic pressure. While other factors like food availability and predator avoidance are important, the deep sea organisms must have the ability to maintain well-regulated metabolic system in the face of high pressures. [1] In order to adjust for the extreme environment, these organisms have developed unique characteristics.
Proteins are affected greatly by the elevated hydrostatic pressure, as they undergo changes in water organization during hydration and dehydration reactions of the binding events. This is due to the fact that most enzyme-ligand interactions form through charged or polar non-charge interactions. Because hydrostatic pressure affects both protein folding and assembly and enzymatic activity, the deep sea species must undergo physiological and structural adaptations to preserve protein functionality against pressure.[1][2]
Actin is a protein that is essential for different cellular functions. The α-actin serves as a main component for muscle fiber, and it is highly conserved across numerous different species. Some Deep-sea fish developed pressure tolerance through the change in mechanism of their α-actin. In some species that live in depths greater than 5000m, C.armatus and C.yaquinae have specific substitutions on the active sites of α-Actin, which serves as the main component of muscle fiber.[3] These specific substitutions, Q137K and V54A from C.armatus or I67P from C.yaquinae are predicted to have importance in pressure tolerance.[3] Substitution in the active sites of actin result in significant changes in the salt bridge patterns of the protein, which allows for better stabilization in ATP binding and sub unit arrangement, confirmed by the free energy analysis and molecular dynamics simulation.[4] It was found that deep sea fish have more salt bridges in their actins compared to fish inhabiting the upper zones of the sea.[3]
In relations to protein substitution, specific osmolytes were found to be abundant in deep sea fish under high hydrostatic pressure. For certain chondrichtyans, it was found that Trimethylamine N-oxide (TMAO) increased with depth, replacing other osmolytes and urea.[5] Due to the ability of TMAO being able to protect proteins from high hydrostatic pressure destabilizing proteins, the osmolyte adjustment serves are an important adaptation for deep sea fish to withstand high hydrostatic pressure.
Deep sea organisms possess molecular adaptations to survive and thrive in the deep oceans. Mariana hadal snailfish developed modification in the Osteocalcin(bglap) gene, where premature termination of the gene was found.[2] Osteocalcin gene regulates bone development and tissue mineralization, and the frameshift mutation seem to have resulted in open skull and cartilage-based bone formation.[2] Due to high hydrostatic pressure in the deep sea, closed skulls that organisms living on the surface develop cannot withstand the enforcing stress. Similarly, common bone developments seen in surface vertebrates cannot maintain its structural integrity under constant high pressure.[2]
Citations[edit]
- ^ a b "Chapter Twelve. Adaptations to the Deep Sea", Biochemical Adaptation, Princeton University Press, pp. 450–495, 1984-12-31, ISBN 978-1-4008-5541-4, retrieved 2020-11-02
- ^ a b c d Wang, Kun; Shen, Yanjun; Yang, Yongzhi; Gan, Xiaoni; Liu, Guichun; Hu, Kuang; Li, Yongxin; Gao, Zhaoming; Zhu, Li; Yan, Guoyong; He, Lisheng (2019-05). "Morphology and genome of a snailfish from the Mariana Trench provide insights into deep-sea adaptation". Nature Ecology & Evolution. 3 (5): 823–833. doi:10.1038/s41559-019-0864-8. ISSN 2397-334X.
{{cite journal}}: Check date values in:|date=(help) - ^ a b c Wakai, Nobuhiko; Takemura, Kazuhiro; Morita, Takami; Kitao, Akio (2014-01-20). "Mechanism of Deep-Sea Fish α-Actin Pressure Tolerance Investigated by Molecular Dynamics Simulations". PLOS ONE. 9 (1): e85852. doi:10.1371/journal.pone.0085852. ISSN 1932-6203. PMC 3896411. PMID 24465747.
{{cite journal}}: CS1 maint: PMC format (link) CS1 maint: unflagged free DOI (link) - ^ Hata, Hiroaki; Nishiyama, Masayoshi; Kitao, Akio (2020-02-01). "Molecular dynamics simulation of proteins under high pressure: Structure, function and thermodynamics". Biochimica et Biophysica Acta (BBA) - General Subjects. Novel measurement techniques for visualizing 'live' protein molecules. 1864 (2): 129395. doi:10.1016/j.bbagen.2019.07.004. ISSN 0304-4165.
- ^ Yancey, Paul H.; Speers-Roesch, Ben; Atchinson, Sheila; Reist, James D.; Majewski, Andrew R.; Treberg, Jason R. (2017-11-27). "Osmolyte Adjustments as a Pressure Adaptation in Deep-Sea Chondrichthyan Fishes: An Intraspecific Test in Arctic Skates (Amblyraja hyperborea) along a Depth Gradient". Physiological and Biochemical Zoology. 91 (2): 788–796. doi:10.1086/696157. ISSN 1522-2152.