PMID:11886743
| Citation |
Rosen, R, Biran, D, Gur, E, Becher, D, Hecker, M and Ron, EZ (2002) Protein aggregation in Escherichia coli: role of proteases. FEMS Microbiol. Lett. 207:9-12 |
|---|---|
| Abstract |
Protein aggregation is involved in several human diseases, and presumed to be an important process in protein quality control. In bacteria, aggregation of proteins occurs during stress conditions, such as heat shock. We studied the protein aggregates of Escherichia coli during heat shock. Our results demonstrate that the concentration and diversity of proteins in the aggregates depend on the availability of proteases. Aggregates obtained from mutants in the Lon (La) protease contain three times more protein than wild-type aggregates and show the broadest protein diversity. The results support the assumption that protein aggregates are formed from partially unfolded proteins that were not refolded by chaperones or degraded by proteases. |
| Links | |
| Keywords |
ATP-Dependent Proteases; Adenosine Triphosphatases/genetics; Adenosine Triphosphatases/metabolism; Endopeptidase Clp; Endopeptidases/genetics; Endopeptidases/metabolism; Escherichia coli/chemistry; Escherichia coli/enzymology; Escherichia coli/genetics; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Gene Deletion; Heat-Shock Proteins/genetics; Heat-Shock Proteins/metabolism; Heat-Shock Response; Protease La; Protein Folding; Proteome; Serine Endopeptidases/genetics; Serine Endopeptidases/metabolism |
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