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The protein folding challenge in psychrophiles: facts and current issues
Author(s) -
Piette Florence,
Struvay Caroline,
Feller Georges
Publication year - 2011
Publication title -
environmental microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.954
H-Index - 188
eISSN - 1462-2920
pISSN - 1462-2912
DOI - 10.1111/j.1462-2920.2011.02436.x
Subject(s) - psychrophile , protein folding , biology , chaperone (clinical) , folding (dsp implementation) , limiting , mesophile , biochemistry , biophysics , microbiology and biotechnology , enzyme , genetics , bacteria , medicine , mechanical engineering , pathology , electrical engineering , engineering
Summary The protein folding process in psychrophiles is impaired by low temperature, which exerts several physicochemical constraints, such as a decrease in the folding rate, reduced molecular diffusion rates and increased solvent viscosity, which interfere with conformational sampling. Furthermore, folding assistance is required at various folding steps according to the protein size. Recent studies in the field have provided contrasting and sometimes contradictory results, although protein folding generally appears as a rate‐limiting step for the growth of psychrophiles. It is proposed here that these discrepancies reflect the diverse adaptive strategies adopted by psychrophiles in order to allow efficient protein folding at low temperature. Cold adaptations apparently superimpose on pre‐existing cellular organization, resulting in different adaptive strategies. In addition, microbial lifestyle further modulates the properties of the chaperone machinery, which possibly explains the occurrence of cold‐adapted and non‐cold‐adapted protein chaperones in psychrophiles.