Research on the effects of exposure of micro-organisms to high hydrostatic pressure (HHP) has grown in the last decade. The main foci have been to understand adaptation to life in the deep ocean and the HHP stress response. Amongst other effects, HHP interferes with the cellular membrane structure, increasing the order of lipid molecules especially in the vicinity of proteins, leading to decreased membrane fluidity. Protein structure may also be affected by pressure, disturbing polymerization, folding and the activity. HHP also inhibits protein synthesis, one of the most piezosensitive cellular functions. Ribosome disassembly contributes to this inhibition. RNA synthesis is maintained at pressures at which DNA and protein synthesis are completely inhibited. A number of these responses overlap with responses to other forms of stress, particularly cold stress. Microarray analysis of micro-organisms has identified numerous genes upregulated after exposure to high pressure. However, many of these genes code for proteins of unknown function. Corresponding proteomic analyses detect very few proteins synthesized as a result of such exposure. The review high lights the need for future research to understand the complex pathways involved in the response to HHP.
Keywords: Piezophile, piezotolerant, proteomic, pressure-inducible proteins, cold stress, heat shock
Rights & PermissionsPrintExport