Divergent genetic control of protein solubility and conformational quality in Escherichia coli.

doi:10.1016/j.jmb.2007.09.004

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Article

Divergent genetic control of protein solubility and conformational quality in Escherichia coli.

Journal of molecular biology - 16 Nov 2007

García-Fruitós Elena, Martínez-Alonso Mónica, Gonzàlez-Montalbán Nuria, Valli Minoska, Mattanovich Diethard, Villaverde Antonio

Abstract excerpt

In bacteria, protein overproduction results in the formation of inclusion bodies, sized protein aggregates showing amyloid-like properties such as seeding-driven formation, amyloid-tropic dye binding, intermolecular beta-sheet architecture and cytotoxicity on mammalian cells. During protein deposition, exposed hydrophobic patches force intermolecular clustering and aggregation but these aggregation determinants...

Topics

Cytosol
Escherichia coli
Escherichia coli Proteins
HSP70 Heat-Shock Proteins
Heat-Shock Response
Inclusion Bodies
Molecular Chaperones
Mutation
Protein Denaturation
Protein Folding
Protein Structure, Secondary
Solubility

Source

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Identifiers

PMID: 17920630
DOI: 10.1016/j.jmb.2007.09.004

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