Abstract The role of various interactions in determining the pressure adaptation of the proteome in piezophilic organisms remains to be established. It is clear that the adaptation is not limited to one or two proteins, but has a more general evolution of the characteristics of the entire proteome, the so-called cryptic evolution. Using the synergy between bioinformatics, computer simulations, and some experimental evidence, we probed the physico-chemical mechanisms of cryptic evolution of the proteome of psychrophilic strains of model organism,Colwellia, to adapt to life at various pressures, from the surface of the Arctic ice to the depth of the Mariana Trench. From the bioinformatics analysis of proteomes of several strains of Colwellia, we have identified the modulation of interactions between charged residues as a possible driver of evolutionary adaptation to high hydrostatic pressure. The computational modeling suggests that these interactions have different roles in modulating the function-stability relationship for different protein families. For several classes of proteins, the modulation of interactions between charges evolved to lead to an increase in stability with pressure, while for others, just the opposite is observed. The latter trend appears to benefit enzyme activity by countering structural rigidification due to the high pressure. 
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                            Protein adaptation to high hydrostatic pressure: Computational analysis of the structural proteome
                        
                    
    
            Abstract Hydrostatic pressure has a vital role in the biological adaptation of the piezophiles, organisms that live under high hydrostatic pressure. However, the mechanisms by which piezophiles are able to adapt their proteins to high hydrostatic pressure is not well understood. One proposed hypothesis is that the volume changes of unfolding (ΔVTot) for proteins from piezophiles is distinct from those of nonpiezophilic organisms. Since ΔVTotdefines pressure dependence of stability, we performed a comprehensive computational analysis of this property for proteins from piezophilic and nonpiezophilic organisms. In addition, we experimentally measured the ΔVTotof acylphosphatases and thioredoxins belonging to piezophilic and nonpiezophilic organisms. Based on this analysis we concluded that there is no difference in ΔVTotfor proteins from piezophilic and nonpiezophilic organisms. Finally, we put forward the hypothesis that increased concentrations of osmolytes can provide a systemic increase in pressure stability of proteins from piezophilic organisms and provide experimental thermodynamic evidence in support of this hypothesis. 
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                            - Award ID(s):
 - 1803045
 
- PAR ID:
 - 10457226
 
- Publisher / Repository:
 - Wiley Blackwell (John Wiley & Sons)
 
- Date Published:
 
- Journal Name:
 - Proteins: Structure, Function, and Bioinformatics
 
- Volume:
 - 88
 
- Issue:
 - 4
 
- ISSN:
 - 0887-3585
 
- Page Range / eLocation ID:
 - p. 584-592
 
- Format(s):
 - Medium: X
 
- Sponsoring Org:
 - National Science Foundation
 
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