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Protein folding and aggregation in bacteria

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Abstract

Proteins might experience many conformational changes and interactions during their lifetimes, from their synthesis at ribosomes to their controlled degradation. Because, in most cases, only folded proteins are functional, protein folding in bacteria is tightly controlled genetically, transcriptionally, and at the protein sequence level. In addition, important cellular machinery assists the folding of polypeptides to avoid misfolding and ensure the attainment of functional structures. When these redundant protective strategies are overcome, misfolded polypeptides are recruited into insoluble inclusion bodies. The protein embedded in these intracellular deposits might display different conformations including functional and β-sheet-rich structures. The latter assemblies are similar to the amyloid fibrils characteristic of several human neurodegenerative diseases. Interestingly, bacteria exploit the same structural principles for functional properties such as adhesion or cytotoxicity. Overall, this review illustrates how prokaryotic organisms might provide the bedrock on which to understand the complexity of protein folding and aggregation in the cell.

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Acknowledgments

Work in our laboratory has been supported by grants BIO2007-68046 (Ministerio de Ciencia e Innovación, Spain) and 2009-SGR-760 (Generalitat de Catalunya).

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  1. Departament de Bioquímica i Biologia Molecular, Institut de Biotecnologia i de Biomedicina, Universitat Autònoma de Barcelona, 08193, Bellaterra, Barcelona, Spain

    Raimon Sabate, Natalia S. de Groot & Salvador Ventura

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  1. Raimon Sabate
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  2. Natalia S. de Groot
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  3. Salvador Ventura
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Correspondence to Salvador Ventura.

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R. Sabate and N. S. de Groot contributed equally to this work.

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Sabate, R., de Groot, N.S. & Ventura, S. Protein folding and aggregation in bacteria. Cell. Mol. Life Sci. 67, 2695–2715 (2010). https://doi.org/10.1007/s00018-010-0344-4

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