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PMID:15866952
| Citation |
Carrió, MM and Villaverde, A (2005) Localization of chaperones DnaK and GroEL in bacterial inclusion bodies. J. Bacteriol. 187:3599-601 |
|---|---|
| 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. |
| Links |
PubMed PMC1111989 Online version:10.1128/JB.187.10.3599-3601.2005 |
| Keywords |
Chaperonin 60/metabolism; Escherichia coli/metabolism; Escherichia coli/ultrastructure; Escherichia coli Proteins/metabolism; HSP70 Heat-Shock Proteins/metabolism; Inclusion Bodies/metabolism; Inclusion Bodies/ultrastructure; Microscopy, Immunoelectron |
Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0071218: cellular response to misfolded protein |
ECO:0000314: |
P |
Figure 1. Shows a cellular response to misfolded protein aggregation via localization of the GroEL chaperone system to the β-galactosidase fusion protein VP1LAC aggreagate in the cytoplasm |
complete | ||||
| GO:0005737: cytoplasm |
ECO:0000314: |
C |
Figure 1. shows GroEl chaperone system localization to aggregation-prone β-galactosidase fusion protein VP1LAC in the cytoplasm. |
complete | ||||
| GO:0016234: cytoplasm |
ECO:0000314: |
C |
Figure 1. Shows strong Dnak chaperone system localization to the inclusion body surfaces of fusion protein VP1LAC while low levels were detected in the cytoplasm. |
complete | ||||
Notes
See also
References
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