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FEBS Lett. 2006 Nov 27;580(27):6471-6. Epub 2006 Nov 10.

Effect of temperature on protein quality in bacterial inclusion bodies.

Author information

1
Departament de Bioquímica i Biologia Molecular, Universitat Autònoma de Barcelona, E-08193 Bellaterra, Spain.

Abstract

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 Abeta42 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.

PMID:
17101131
DOI:
10.1016/j.febslet.2006.10.071
[Indexed for MEDLINE]
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