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- W2511793582 abstract "Escherichia coli ion mutants are defective in the ATP-dependent proteolysis of abnormal proteins. The mutants are also sensitive to ultraviolet light (UV) in that septation is in- hibited after exposure to UV. sulA mutations, isolated as sup- pressors of UV sensitivity unlinked to ion, do not affect proteolysis but allow septation to occur after DNA damage. We have con- firmed the hypothesis that the product of the sulA gene is degraded by lon proteolysis. If sulA (the product of sulA) is a UV-inducible division inhibitor, as suggested by a variety of experiments, Ion (the product of lon) may regulate cell division by regulating the half-life of sulA. We cloned the sulA gene in a bacteriophage A vector from a plasmid carrying the ompA region of E. coli. An 18- kilodalton polypeptide was identified as the product of the sulA gene. Pulse-chase labeling demonstrated that the half-life of the sulA protein is 1.2 min in lon+ cells and 19 min in lon- cells. This work demonstrates that Ion proteolysis affects the stability of a native E. coli protein." @default.
- W2511793582 created "2016-09-16" @default.
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- W2511793582 date "2016-01-01" @default.
- W2511793582 modified "2023-09-24" @default.
- W2511793582 title "Protein degradation in Escherichia , stability of sulA protein" @default.
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- W2511793582 hasPublicationYear "2016" @default.
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