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. 2005 May;187(10):3599-601.
doi: 10.1128/JB.187.10.3599-3601.2005.

Localization of chaperones DnaK and GroEL in bacterial inclusion bodies

M Mar Carrió  1 , Antonio Villaverde
Affiliations

Localization of chaperones DnaK and GroEL in bacterial inclusion bodies

M Mar Carrió et al. J Bacteriol. 2005 May.

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.

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Figures

FIG. 1.
FIG. 1.
In situ immunodetection of DnaK (A, B, C), GroEL (D, E, F), and β-galactosidase (J, K) in E. coli cells producing the inclusion body-forming protein VP1LAC. Double-detection images of DnaK (15-nm gold particles) and GroEL (10-nm gold particles) on VP1LAC-producing cells (G, H) and those expressing the parental, soluble beta-galactosidase (I) are also shown. Cells incubated only with the secondary anti-rabbit antibody (BBInternational EMGAR-10) are also shown as a control of the procedure (L). Horizontal bars depicted in the panels represent 200 nm.
See this image and copyright information in PMC

References

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