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Pressure-tolerant Evolution in Rhodopsin of Deep-diving Whales.

Hayate Takeuchi1, Takashi Hayakawa2

  • 1Graduate School of Environmental Science, Hokkaido University, Sapporo, Hokkaido, Japan.

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Summary

Deep-diving whales possess specialized rhodopsin proteins that maintain visual function under extreme hydrostatic pressure. This adaptation involves specific amino acid changes, enhancing protein stability and resilience in the deep sea.

Keywords:
cetaceancodon substitution modeldeep-seahydrostatic pressuremolecular dynamicsvision

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Area of Science:

  • Marine Biology
  • Molecular Evolution
  • Biophysics

Background:

  • Deep-sea life poses extreme challenges to protein structure and function due to hydrostatic pressure.
  • Cetacean rhodopsins are adapted for underwater light, but pressure adaptations remain unexplored.

Purpose of the Study:

  • To investigate structural modifications in cetacean rhodopsin for deep-diving visual function.
  • To identify evolutionary adaptations of rhodopsin to extreme hydrostatic pressure.

Main Methods:

  • Physicochemical property-based codon substitution modeling to identify amino acid changes.
  • Molecular dynamics simulations to assess protein stability and flexibility under pressure.

Main Results:

  • Amino acid replacements favoring altered compressibility were found in deep-diving cetaceans (Physeteroidea, Ziphiidae).
  • Alanine at residue 2997.46a enhances rhodopsin pressure tolerance, showing lower compressibility and flexibility.
  • Molecular simulations confirmed reduced free-energy costs for alanine under high pressure.

Conclusions:

  • Residue 2997.46a is a key site for pressure adaptation in deep-diving cetacean rhodopsins.
  • Cetacean rhodopsins evolved for both spectral sensitivity and structural resilience under pressure.
  • Integrative approach advances understanding of protein adaptation in extreme environments.