Localization of Chaperones DnaK and GroEL in Bacterial Inclusion Bodies

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.

[1]  J. Corchero,et al.  Limited in vivo proteolysis of aggregated proteins. , 1997, Biochemical and biophysical research communications.

[2]  P. Valax,et al.  Molecular Characterization of β‐Lactamase Inclusion Bodies Produced in Escherichia coli. 1. Composition , 1993, Biotechnology progress.

[3]  P Neubauer,et al.  Monitoring of genes that respond to overproduction of an insoluble recombinant protein in Escherichia coli glucose-limited fed-batch fermentations. , 2000, Biotechnology and bioengineering.

[4]  A. Villaverde,et al.  Construction and deconstruction of bacterial inclusion bodies. , 2002, Journal of biotechnology.

[5]  Antonio Villaverde,et al.  Role of molecular chaperones in inclusion body formation , 2003, FEBS letters.

[6]  J. Corchero,et al.  Proteolytic digestion of bacterial inclusion body proteins during dynamic transition between soluble and insoluble forms. , 1999, Biochimica et biophysica acta.

[7]  F. Baneyx,et al.  Influence of the GroE molecular chaperone machine on the in vitro refolding of Escherichia coli β‐galactosidase , 1996, Protein science : a publication of the Protein Society.

[8]  Jimena Weibezahn,et al.  Unscrambling an egg: protein disaggregation by AAA+ proteins , 2004, Microbial cell factories.

[9]  G. Georgiou,et al.  Isolating inclusion bodies from bacteria. , 1999, Methods in enzymology.

[10]  J. Corchero,et al.  Dynamics of in vivo protein aggregation: building inclusion bodies in recombinant bacteria. , 1998, FEMS microbiology letters.

[11]  J. Bailey,et al.  Overexpression of bacterial hemoglobin causes incorporation of pre-beta-lactamase into cytoplasmic inclusion bodies , 1993, Applied and environmental microbiology.

[12]  J. Betton,et al.  Protein quality control in the bacterial periplasm , 2004, Microbial cell factories.

[13]  J. Corchero,et al.  Distinct chaperone affinity to folding variants of homologous recombinant proteins , 1999, Biotechnology Letters.

[14]  James E. Bailey,et al.  Protein compositional analysis of inclusion bodies produced in recombinant Escherichia coli , 1992, Applied Microbiology and Biotechnology.

[15]  A. Villaverde,et al.  Protein aggregation as bacterial inclusion bodies is reversible , 2001, FEBS letters.

[16]  G. Farr,et al.  GroEL/GroES-Mediated Folding of a Protein Too Large to Be Encapsulated , 2001, Cell.

[17]  A. Villaverde,et al.  Protein aggregation in recombinant bacteria: biological role of inclusion bodies , 2003, Biotechnology Letters.

[18]  F. Baneyx,et al.  Recombinant protein folding and misfolding in Escherichia coli , 2004, Nature Biotechnology.

[19]  J. Bailey,et al.  Characterization of inclusion bodies in recombinant Escherichia coli producing high levels of porcine somatotropin. , 1993, Journal of biotechnology.