Potential use of toxic thermolabile proteins to study protein quality control systems.
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.
Mizrahi
Itzhak
I
Department of Molecular Microbiology and Biotechnology, Life Sciences, Tel Aviv University, Tel Aviv, Israel 69978.
Dagan
Michael
M
Biran
Dvora
D
Ron
Eliora Z
EZ
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
D003598:Cytoskeletal Proteins; D029968:Escherichia coli Proteins; C053139:sulA protein, E coli