@article{0cf5be3e49584c2faa87f9b40a58cd65,
title = "Protein aggregation in Escherichia coli: Role of proteases",
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.",
keywords = "ClpP protease, Heat shock, HslVU protease, Lon (La) protease",
author = "Ran Rosen and Dvora Biran and Eyal Gur and D{\"o}rte Becher and Michael Hecker and Ron, {Eliora Z.}",
note = "Funding Information: We thank Knut B{\"u}ttner for critical reading of the manuscript and for excellent suggestions. This work was partially supported by a Colton Scholarship (R.R.) and by the Manja and Morris Leigh Chair (E.Z.R.) for Biophysics and Biotechnology. ",
year = "2002",
month = jan,
day = "22",
doi = "10.1016/S0378-1097(01)00557-2",
language = "אנגלית",
volume = "207",
pages = "9--12",
journal = "FEMS Microbiology Letters",
issn = "0378-1097",
publisher = "Oxford University Press",
number = "1",
}