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Effect of temperature on protein quality in bacterial inclusion bodies
Author(s) -
de Groot Natalia Sánchez,
Ventura Salvador
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.10.071
Subject(s) - proteolysis , inclusion bodies , denaturation (fissile materials) , protein folding , protein aggregation , biophysics , chemistry , peptide , recombinant dna , biochemistry , microbiology and biotechnology , biology , enzyme , nuclear chemistry , gene
Increasing evidence indicates that protein aggregation in bacteria does not necessarily imply loss of biological activity. Here, we have investigated the effect of growth‐temperature on both the activity and stability of the inclusion bodies formed by a point‐mutant of Aβ42 Alzheimer peptide, using green fluorescent protein as a reporter. The activity in the aggregates inversely correlates with the temperature. In contrast, inclusion bodies become more stable in front of chemical denaturation and proteolysis when temperature increases. Overall, the data herein open new perspectives in protein production, while suggesting a kinetic competition between protein folding and aggregation during recombinant protein expression.