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Concepts and tools to exploit the potential of bacterial inclusion bodies in protein science and biotechnology
Author(s) -
GattiLafranconi Pietro,
Natalello Antonino,
Ami Diletta,
Doglia Silvia Maria,
Lotti Marina
Publication year - 2011
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/j.1742-4658.2011.08163.x
Subject(s) - inclusion bodies , protein folding , protein aggregation , computational biology , cytoplasm , biology , folding (dsp implementation) , protein engineering , microbiology and biotechnology , recombinant dna , biochemistry , gene , engineering , electrical engineering , enzyme
Cells have evolved complex and overlapping mechanisms to protect their proteins from aggregation. However, several reasons can cause the failure of such defences, among them mutations, stress conditions and high rates of protein synthesis, all common consequences of heterologous protein production. As a result, in the bacterial cytoplasm several recombinant proteins aggregate as insoluble inclusion bodies. The recent discovery that aggregated proteins can retain native‐like conformation and biological activity has opened the way for a dramatic change in the means by which intracellular aggregation is approached and exploited. This paper summarizes recent studies towards the direct use of inclusion bodies in biotechnology and for the detection of bottlenecks in the folding pathways of specific proteins. We also review the major biophysical methods available for revealing fine structural details of aggregated proteins and which information can be obtained through these techniques.