Properties of ATPase Activity of ATP-dependent Clp Protease in Escherichia coli

Escherichia coli내의 ATP-dependent Clp효소의 ATPase 활성 연구

  • ;
  • Michael R. Maurizi
  • 김승호 (한국과학기술연구원 유전공학연구소 단백질화학연구실) ;
  • Published : 1993.02.01


Clp is a relatively abundant ATP-dependent protease found in E. coli. Its specific activity was proportional to the concentration of the limiting amount of Clp A and an excess amount of Clp P, and vice versa. Clp A has an intrinsic ATPase activity that is stimulated by casein, and contains a second site for binding A TP, in addition to the ATPase site. The modification of sulfhydryl groups in Clp A with reagents which have bulky groups such as N-phenylmaleimide led to nullifying both ATPase and protease activity. The same sites were modified by sulfhydryl reagents. It seems that the sulfhydryl groups of Clp A are not directly involved in catalysis. Since non-hydrolyzable analogs of ATP do not activate Clp, ATP hydrolysis may be essential for the proteolytic activity of Clp protease. Clp A and Clp P did not associate in the absence of nucleotide. The results suggest that the activity of the proteolytic component, Clp P, is regulated by the A TP-dependent cycling of Clp A between the activator form and the non-activator form.


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