Year: 2022
Type: article
Abstract: Life is thought to have appeared in the depth of the sea under high hydrostatic pressure. Nowadays, it is known that the deep biosphere hosts a myriad of life forms thriving under high-pressure conditions. However, the evolutionary mechanisms leading to their adaptation are still not known. Here, we show the molecular bases of these mechanisms through a joint structural and dynamical study of two orthologous proteins. We observed that pressure adaptation involves the decoupling of protein-water dynamics and the elimination of cavities in the protein core. This is achieved by rearranging the charged residues on the protein surface and using bulkier hydrophobic residues in the core. These findings will be the starting point in the search for a complete genomic model explaining high-pressure adaptation.
DOI: 10.3390/ijms23158469
Institutions: Lyon 1 Université, Centre National de la Recherche Scientifique, Université de Lyon, Laboratoire de Microbiologie, Adaptation et Pathogénie, Institut National des Sciences Appliquées de Lyon, Inserm, Université de Montpellier, Centre de Biologie Structurale, Institut Laue-Langevin, Institut Universitaire de France, Laboratoire Interdisciplinaire de Physique, Université Grenoble Alpes
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: gold
Estimated APC paid: $2,408
OpenAlex ID: W4289175460