The effect of co-overproduction of DnaK/DnaJ/GrpE and ClpB proteins on the removal of heat-aggregated proteins from Escherichia coli ΔclpB mutant cells - New insight into the role of Hsp70 in a functional cooperation with Hsp100

FEMS Microbiology Letters

Volumn 204, Issue 2, 2001, Pages 355-360

  Kedzierska, Sabina ^a   Matuszewska, Ewelina ^a  

^a UNIVERSITY OF GDA SK   (Poland)

Author keywords

Escherichia coli; Heat shock protein; Heat aggregated protein; Removal of the aggregate; S fraction

Indexed keywords

BACTERIAL PROTEIN; HEAT SHOCK PROTEIN 100; HEAT SHOCK PROTEIN 70; MUTANT PROTEIN; PROTEIN CLPB; PROTEIN DNAJ; PROTEIN DNAK; PROTEIN GRPE; UNCLASSIFIED DRUG;

ARTICLE; BACTERIUM CULTURE; BACTERIUM MUTANT; CELL MUTANT; CONTROLLED STUDY; ESCHERICHIA COLI; GENE MUTATION; HEAT SHOCK; NONHUMAN; PRIORITY JOURNAL; PROMOTER REGION; PROTEIN AGGREGATION; PROTEIN EXPRESSION; SUCROSE DENSITY GRADIENT CENTRIFUGATION;

BACTERIAL PROTEINS; CENTRIFUGATION, DENSITY GRADIENT; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; GENE EXPRESSION REGULATION, BACTERIAL; HEAT-SHOCK PROTEINS; HEAT-SHOCK RESPONSE; HSP40 HEAT-SHOCK PROTEINS; HSP70 HEAT-SHOCK PROTEINS; PLASMIDS; PROTEIN RENATURATION; PROTOZOAN PROTEINS;

ESCHERICHIA COLI;

EID: 0035856592     PISSN: 03781097     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1097(01)00427-X     Document Type: Article

References (22)

1. Response of Escherichia coli cell membranes to induction of λ cI857 prophage by heat shock
2. The heat shock response of Escherichia coli
3. Heat-inactivated proteins are rescued by the DnaKJ-GrpE set and ClpB chaperones
4. ClpB cooperates with Dank, DnaJ, and GrpE in suppressing protein aggregation
5. Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network
6. Identification of thermolabile Escherichia coli proteins: Prevention and reversion of aggregation by DnaK and ClpB
7. Hsp104, Hsp70, and Hsp40: A novel chaperone system that rescues previously aggregated proteins
8. The heat-shock protein ClpB in Escherichia coli is a protein-activated ATPase
9. ClpB is the Escherichia coli heat shock protein F84.1
10. Degradation by proteases Lon, Clp and HtrA, of Escherichia coli proteins aggregated in vivo by heat shock; HtrA protease action in vivo and in vitro
11. Dnak/DnaJ chaperone system reactivates endogrnous E. coli thermostable FBP aldolase in vivo and in vitro; the effect is enhanced by GroE heat shock proteins
12. The role of DnaK/DnaJ and GroEL/GroES systems in the removal of endogenous proteins aggregated by heat shock from Escherichia coli cells
13. Sequence and structure of ClpP, the proteolytic component of the ATP-dependent Clp protease of Escherichia coli
14. Chaperone coexpression plasmids: Differential and synergistic roles of DnaK-DnaJ-GrpE and GroEL-GroES in assisting folding of an allergen of japanese cedar pollen, Cryj2, in Escherichia coli
15. The effect of some antibiotic-resistance-conferring plasmids on the removal of the heat-aggregated proteins from Escherichia coli cells
16. An efficient and reproducible procedure for the formation of spheroplasts from variously grown Escherichia coli
17. A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
18. Cleavage of structural proteins during assembly of the head of bacteriophage T4
19. Fluorescent staining of proteins transferred to nitrocellulose allowing for subsequent probing with antisera
20. Protein aggregation and inclusion body formation in Escherichia coli rpoH mutant defective in heat-shock protein induction