Protein quality in bacterial inclusion bodies.
A common limitation of recombinant protein production in bacteria is the formation of insoluble protein aggregates known as inclusion bodies. The propensity of a given protein to aggregate is unpredictable, and the goal of a properly folded, soluble species has been pursued using four main approaches: modification of the protein sequence; increasing the availability of folding assistant proteins; increasing the performance of the translation machinery; and minimizing physicochemical conditions favoring conformational stress and aggregation. From a molecular point of view, inclusion bodies are considered to be formed by unspecific hydrophobic interactions between disorderly deposited polypeptides, and are observed as "molecular dust-balls" in productive cells. However, recent data suggest that these protein aggregates might be a reservoir of alternative conformational states, their formation being no less specific than the acquisition of the native-state structure.
Ventura
Salvador
S
Institut de Biotecnologia i de Biomedicina, Universitat Autònoma de Barcelona, Bellaterra, 08193 Barcelona, Spain.
Villaverde
Antonio
A
D001426:Bacterial Proteins / Q000032:analysis* / Q000737:chemistry*; D002479:Inclusion Bodies / Q000737:chemistry*; D017510:Protein Folding; D011994:Recombinant Proteins / Q000032:analysis / Q000737:chemistry; D020539:Sequence Analysis, Protein
D001426:Bacterial Proteins; D011994:Recombinant Proteins