Localization of Chaperones DnaK and GroEL in Bacterial Inclusion Bodies-Reference-Cited by-同舟云学术

Localization of Chaperones DnaK and GroEL in Bacterial Inclusion Bodies

Published:2005-05-15 Issue:10 Volume:187 Page:3599-3601
ISSN:0021-9193
Container-title:Journal of Bacteriology
language:en
Short-container-title:J Bacteriol

Author:

Carrió M. Mar¹,Villaverde Antonio¹

Affiliation:

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

Abstract

ABSTRACT By immunostaining and transmission electron microscopy, chaperones DnaK and GroEL have been identified at the solvent-exposed surface of bacterial inclusion bodies and entrapped within these aggregates, respectively. Functional implications of this distinct localization are discussed in the context of Escherichia coli protein quality control.

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

Link

https://journals.asm.org/doi/pdf/10.1128/JB.187.10.3599-3601.2005

Reference19 articles.

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3. Boels, K., M. M. Carrió, A. Arís, J. L. Corchero, and A. Villaverde. 1999. Distinct chaperone affinity to folding variants of homologous recombinant proteins. Biotechnol. Lett.21:531-536.

4. Carrio, M. M., J. L. Corchero, and A. Villaverde. 1998. Dynamics of in vivo protein aggregation: building inclusion bodies in recombinant bacteria. FEMS Microbiol. Lett.169:9-15.

5. Carrio, M. M., J. L. Corchero, and A. Villaverde. 1999. Proteolytic digestion of bacterial inclusion body proteins during dynamic transition between soluble and insoluble forms. Biochim. Biophys. Acta1434:170-176.

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