Proteolysis and modulation of the activity of the cell division inhibitor SulA in Escherichia coli lon mutants.
Intracellular accumulation of the inducible cell division inhibitor SulA is modulated by proteases that ensure its degradation, namely, the Lon protease and another ATP-dependent protease(s). Lon- cells are UV sensitive because SulA is stable. We asked whether these ATP-dependent proteases are more active when lon cells are grown at high temperature or in synthetic medium since these conditions decrease the UV sensitivity of lon cells. We found that these growth conditions have no direct effect on Lon-independent degradation of SulA. They may, instead, decrease the SulA-FtsZ interaction.
Canceill
D
D
Département de Biotechnologie, Institut Pasteur, Paris, France.
Dervyn
E
E
Huisman
O
O
D049069:ATP-Dependent Proteases; D001426:Bacterial Proteins / Q000378:metabolism*; D002455:Cell Division; D004734:Energy Metabolism; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism*; D029968:Escherichia coli Proteins; D006360:Heat-Shock Proteins; D009154:Mutation; D049070:Protease La; D012697:Serine Endopeptidases / Q000378:metabolism*; D013696:Temperature
D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D006360:Heat-Shock Proteins; C053139:sulA protein, E coli; D049069:ATP-Dependent Proteases; D012697:Serine Endopeptidases; C483567:Lon protein, E coli; D049070:Protease La