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Applied and Environmental Microbiology, January 2007, p. 289-294, Vol. 73, No. 1
0099-2240/07/$08.00+0     doi:10.1128/AEM.01952-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Localization of Functional Polypeptides in Bacterial Inclusion Bodies{triangledown}

Elena García-Fruitós, Anna Arís, and Antonio Villaverde*

Institut de Biotecnologia i de Biomedicina and Departament de Genètica i de Microbiologia, Universitat Autònoma de Barcelona, Bellaterra, 08193 Barcelona, Spain

Received 17 August 2006/ Accepted 21 October 2006

Bacterial inclusion bodies, while showing intriguing amyloid-like features, such as a ß-sheet-based intermolecular organization, binding to amyloid-tropic dyes, and origin in a sequence-selective deposition process, hold an important amount of native-like secondary structure and significant amounts of functional polypeptides. The aggregation mechanics supporting the occurrence of both misfolded and properly folded protein is controversial. Single polypeptide chains might contain both misfolded stretches driving aggregation and properly folded protein domains that, if embracing the active site, would account for the biological activities displayed by inclusion bodies. Alternatively, soluble, functional polypeptides could be surface adsorbed by interactions weaker than those driving the formation of the intermolecular ß-sheet architecture. To explore whether the fraction of properly folded active protein is a natural component or rather a mere contaminant of these aggregates, we have explored their localization by image analysis of inclusion bodies formed by green fluorescent protein. Since the fluorescence distribution is not homogeneous and the core of inclusion bodies is particularly rich in active protein forms, such protein species cannot be passively trapped components and their occurrence might be linked to the reconstruction dynamics steadily endured in vivo by such bacterial aggregates. Intriguingly, even functional protein species in inclusion bodies are not excluded from the interface with the solvent, probably because of the porous structure of these particular protein aggregates.

* Corresponding author. Mailing address: Institut de Biotecnologia i de Biomedicina, Universitat Autònoma de Barcelona, Bellaterra, 08193 Barcelona, Spain. Phone: 34 935812148. Fax: 34 935812011. E-mail: avillaverde{at}servet.uab.es.

{triangledown} Published ahead of print on 3 November 2006.

Applied and Environmental Microbiology, January 2007, p. 289-294, Vol. 73, No. 1
0099-2240/07/$08.00+0     doi:10.1128/AEM.01952-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Martinez-Alonso, M., Gonzalez-Montalban, N., Garcia-Fruitos, E., Villaverde, A. (2008). The Functional Quality of Soluble Recombinant Polypeptides Produced in Escherichia coli Is Defined by a Wide Conformational Spectrum. Appl. Environ. Microbiol. 74: 7431-7433 [Abstract] [Full Text]  


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