Systems-level analysis of protein quality in inclusion body-forming Escherichia coli cells

Elena García-Fruitós, Nuria González-Montalbán, Mónica Martínez-Alonso, Ursula Rinas, Antonio Villaverde

Research output: Chapter in BookChapterResearchpeer-review

Abstract

Recombinant proteins produced in Escherichia coli often aggregate as amorphous masses of insoluble material known as inclusion bodies. Being quite homogeneous in their composition, inclusion bodies display amyloid-like properties such as sequence-dependent protein-protein interactions, seeding-driven deposition of their components and β-sheet intermolecular architecture. However, inclusion bodies formed by different proteins and enzymes also show important extents of native-like secondary structure and include significant proportions of properly folded, functional protein, which makes them suitable to be used in catalytic processes. Inclusion bodies are formed as a result of the incapability of the quality control cell system to cope with the non physiological amounts of misfolding-prone proteins produced upon recombinant gene expression. Multiple cellular proteins involved in the quality control, namely chaperones and proteases, participate in their formation and co-ordinately determine the amount of aggregated protein, the size of aggregates and the main structural and functional properties of the embedded polypeptides, such as their inner molecular organization. © 2009 Springer Netherlands.
Original languageEnglish
Title of host publicationSystems Biology and Biotechnology of Escherichia coli
Pages295-326
Number of pages31
DOIs
Publication statusPublished - 1 Dec 2009

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