This article has been reviewed according to Science X's editorial process and policies. Editors have highlighted the following attributes while ensuring the content's credibility: Life in the deep sea is under immense pressure—literally. Such extreme conditions can disrupt the delicate structures of proteins essential to life.
Yet somehow, the proteins in deep-sea creatures remain functional. This raises an intriguing question: how? A research team led by Professor Gaku Fukuhara of Kyushu University's Institute for Materials Chemistry and Engineering (IMCE) has uncovered a molecular strategy that enables a deep-sea protein to remain stable under extreme pressure.
They found that as pressure increases, the protein assembles into groups of three, called a trimeric structure, and stabilizes itself through a process known as oligomerization-mediated structural stabilization. The findings were published in Scientific Reports on July 8, 2026. "For a long time, no one really understood how organisms adapted to the extreme conditions of the deep sea.
Understanding that adaptation on a molecular level is the motivation behind our study," Fukuhara explains. He designed an experimental study that brought together researchers from different institutions and took a multidisciplinary approach to find the answer. Researchers from the Institute for Solid State Physics at the University of Tokyo prepared the protein samples, while researchers from the Department of Chemistry at the Institute of Science Tokyo executed the experiments.
Together, the team focused on a group of proteins called microbial rhodopsins. Microbial rhodopsins are light-driven proteins, meaning they use light energy to perform biological functions. Although they have been extensively studied under ordinary environmental conditions, far less is known about those originating from extreme environments such as the deep sea.
The researchers compared two microbial rhodopsins from different organisms. The first, Parvularcula oceani xenorhodopsin (PoXeR), is derived from a deep-sea bacterium that has adapted to high-pressure conditions. The second, Gloeobacter rhodopsin (GR), comes from a terrestrial bacterium that normally inhabits atmospheric-pressure environments.
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