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

Abstract

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.

References

  1. FEBS Lett. v.287 Site-directed mutagenesis of La protease Amerik,A.Y.;V.K.Antonov;A.E.Gorbalenya;S.A.Kotova;T.V.Rotanova;E.V.Shimbarevich
  2. J. Bacteriol. v.172 Proteolysis and modulation of the activity of the cell division inhibitor Sul A in Escherichia coli Ion mutants Canceill,D.;E.Dervyn;O.Huisman
  3. Proc. Natl. Acad. Sci. v.78 ATP hydrolysis-dependent activity of the Ion(cap R) protein of E. coli K12 Charette,M.;G.W.Henderson;A.Markovitz
  4. Proc. Natl. Acad. Sci. v.78 The product of the Ion(cap R) gene in Escherichia coli is the ATP-dependent protease, protease La Chung,C.H.;A.L.Goldberg
  5. J. Biol. Chem. v.263 Protease Ti, a new ATP-dependent protease in Escherichia coli contains protein-activated ATPase and proteolytic functions in distinctsubunits Hwang,B.J.;K.M.Woo;A.L.Goldberg;C.H.Chung
  6. J. Biol. Chem. v.262 A multiple-component, ATP-dependent protease from Escherichia coli Katayama,Y.;S.Gottseman;M.R.Maurizi
  7. J. Biol. Chem. v.263 The two-component, ATP-dependent Clp protease of Escherichia coli Katayama,Y.;S.Gottseman;J.Pumphrey;S.Rudikoff;W.P.Clark;M.R.Maurizi
  8. Kor. J. Microbiology v.30 Stability and characterization of the ATP-dependent Clp protease from Escherichia coli Kim,S.H.;M.R.Maurizi
  9. J. Bact. v.164 Insertional mutagenesis of the Ion gene in Escherichia coli: Ion is dispensable Maurizi,M.R.;P.Trisler;S.J.Gottesman
  10. J. Biol. Chem. v.265 Clp Prepresents a unique family of serine proteases Maurizi,M.R.;W.P.Clark;S.H.Kim;S.J.Gottesman
  11. J. Biol. Chem. v.262 Binding of nucleotides to the ATP-dependent protease La from Escherichia coli Menon,A.S.;A.L.Goldberg
  12. Biochim. Biophys. Acta v.542 Studies on the energy requirement for intracellular protein degradation in Escherichia coli Olden,K.;A.L.Goldberg
  13. Proc. Natl. Acad. Sci. USA. v.79 Protease La from Escherichia coli hydrolyzes ATP and proteins in a linked fashion Waxman,L.;A.L.Goldberg
  14. J. Biol. Chem. v.264 Protease Ti from Escherichia coli requires ATP hydrolysis for protein breakdown but not for hydrolysis of small peptides Woo,K.M.;W.J.Chung;D.B.Ha;A.L.Goldberg;C.H.Chung