title: Regulation of activity of an ATP-dependent protease, Clp, by the amount of a subunit, ClpA, in the growth of Escherichia coli cells.
abstract: The activity of an ATP-dependent protease, Clp, was examined in Escherichia coli SG1110 (lon-) in various growth phases. The ATP-dependent proteolytic activity (Clp activity) in a crude extract of the cells changed with the growth phase. Cells in the early exponential growth phase showed the lowest activity, but then the activity increased dramatically with cell growth. The highest Clp activity was found in the cells in the late exponential and early stationary phases, however, the activity returned to the original level on prolonged culturing. These changes in Clp activity were closely correlated to the amount of one of the components of Clp, Clp A, which was quantitated immunochemically with antibodies against the Clp A protein. However, the amount of the other component of Clp, Clp P, did not change with the growth phase. These results suggest that the activity of Clp in the cells is regulated by the amount of Clp A in various growth phases. We next examined the effect of the cellular ATP level on Clp activity, because ATP is a cofactor for Clp protease in vitro. The addition of dinitrophenol (DNP) and sodium azide reduced the intracellular concentration of ATP, but had no effect on the Clp activity or the level of the Clp A protein when these drugs were added to the culture at the stationary phase. On the other hand, these drugs elevated both the Clp activity and the Clp A amount in exponentially growing cells, whose cellular ATP level was also reduced.(ABSTRACT TRUNCATED AT 250 WORDS)
authors.affiliation: Faculty of Agriculture, Tokyo University of Agriculture and Technology.
authors.forename: Y
authors.initials: Y
authors.lastname: Katayama
authors.forename: A
authors.initials: A
authors.lastname: Kasahara
authors.forename: H
authors.initials: H
authors.lastname: Kuraishi
authors.forename: F
authors.initials: F
authors.lastname: Amano
mesh_terms: D049069:ATP-Dependent Proteases; D000255:Adenosine Triphosphate / Q000502:physiology*; D001386:Azides / Q000494:pharmacology; D001426:Bacterial Proteins / Q000378:metabolism; D004140:Dinitrophenols / Q000494:pharmacology; D010450:Endopeptidases / Q000378:metabolism* / Q000502:physiology; D004926:Escherichia coli / Q000187:drug effects / Q000201:enzymology* / Q000254:growth & development; D029968:Escherichia coli Proteins; D006360:Heat-Shock Proteins; D015151:Immunoblotting; D049070:Protease La; D012697:Serine Endopeptidases / Q000502:physiology*; D019810:Sodium Azide; D001616:beta-Galactosidase / Q000378:metabolism
chemical_list: D001386:Azides; D001426:Bacterial Proteins; D004140:Dinitrophenols; D029968:Escherichia coli Proteins; D006360:Heat-Shock Proteins; D000255:Adenosine Triphosphate; D019810:Sodium Azide; D001616:beta-Galactosidase; D010450:Endopeptidases; D049069:ATP-Dependent Proteases; D012697:Serine Endopeptidases; C483567:Lon protein, E coli; D049070:Protease La