Crowding in extremophiles: linkage between solvation and weak protein-protein interactions, stability and dynamics, provides insight into molecular adaptation.
The study of the molecular adaptation of microorganisms to extreme environments (solvent, temperature, etc.) has provided tools to investigate the complex relationships between protein-solvent and protein-protein interactions, protein stability and protein dynamics, and how they are modulated by the crowded environment of the cell. We have evaluated protein-solvent and protein-protein interactions by solution experiments (analytical ultracentrifugation, small angle neutron and X-ray scattering, density) and crystallography, and protein dynamics by energy resolved neutron scattering. This review concerns work from our laboratory on (i) proteins from extreme halophilic Archaea, and (ii) psychrophile, mesophile, thermophile and hyperthermophile bacterial cells.
Ebel
Christine
C
Institut de Biologie Structurale, UMR 5075 CEA-CNRS-UJF, Laboratoire de Biophysique Moléculaire, 41 rue Jules Horowitz, 38027 Grenoble Cedex 1, France. christine.ebel@ibs.fr
Zaccai
Giuseppe
G
D000220:Adaptation, Biological; D019843:Archaeal Proteins / Q000737:chemistry* / Q000378:metabolism; D019614:Haloarcula marismortui / Q000201:enzymology*; D016931:Halobacteriales / Q000737:chemistry / Q000502:physiology; D046911:Macromolecular Substances / Q000737:chemistry / Q000378:metabolism; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D012996:Solutions / Q000737:chemistry; D012997:Solvents / Q000737:chemistry* / Q000378:metabolism
D019843:Archaeal Proteins; D046911:Macromolecular Substances; D011506:Proteins; D012996:Solutions; D012997:Solvents