title: Potential use of toxic thermolabile proteins to study protein quality control systems.
abstract: SulA is an Escherichia coli division inhibitor with a short half-life whose accumulation results in filamentation. Here, we show that SulA is thermally unstable and forms aggregates at elevated temperatures. This property enables the selection of isolates with mutated protein quality control systems.
authors.affiliation: Department of Molecular Microbiology and Biotechnology, Life Sciences, Tel Aviv University, Tel Aviv, Israel 69978.
authors.forename: Itzhak
authors.initials: I
authors.lastname: Mizrahi
authors.forename: Michael
authors.initials: M
authors.lastname: Dagan
authors.forename: Dvora
authors.initials: D
authors.lastname: Biran
authors.forename: Eliora Z
authors.initials: EZ
authors.lastname: Ron
mesh_terms: D002455:Cell Division; D003001:Cloning, Molecular; D003598:Cytoskeletal Proteins; D004926:Escherichia coli / Q000166:cytology / Q000235:genetics / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000378:metabolism; D005798:Genes, Bacterial; D009876:Operon; D013696:Temperature
chemical_list: D003598:Cytoskeletal Proteins; D029968:Escherichia coli Proteins; C053139:sulA protein, E coli