Open AccessProtein aggregation in Escherichia coli : role of proteases
Author(s) -
Rosen Ran,
Biran Dvora,
Gur Eyal,
Becher Dörte,
Hecker Michael,
Ron Eliora Z.
Publication year - 2002
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2002.tb11020.x
Subject(s) - proteases , escherichia coli , protease , protein aggregation , heat shock protein , biochemistry , chemistry , hspa4 , heat shock , mutant , bacteria , enzyme , biology , hsp70 , genetics , gene
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.