Clp-mediated proteolysis in Gram-positive bacteria is autoregulated by the stability of a repressor

EMBO Journal

Volumn 20, Issue 4, 2001, Pages 852-863

  Krüger, Elke ^a   Zühlke, Daniela ^b   Witt, Elke ^a   Ludwig, Holger ^c   Hecker, Michael ^b  

^a CHARITÉ UNIVERSITÄTSMEDIZIN BERLIN   (Germany)

^b UNIVERSITY OF GREIFSWALD   (Germany)

^c UNIVERSITY OF ERLANGEN NUREMBERG   (Germany)

Author keywords

Bacillus subtilis; ClpCP protease; Heat shock; Hsp 100; Proteolysis

Indexed keywords

HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN CLP; PROTEIN KINASE; PROTEIN KINASE MCSA; PROTEIN KINASE MCSB; REPRESSOR PROTEIN; REPRESSOR PROTEIN CTSR; UNCLASSIFIED DRUG;

ARTICLE; BACILLUS SUBTILIS; ESCHERICHIA COLI; HEAT SHOCK RESPONSE; NONHUMAN; NUCLEOTIDE SEQUENCE; OPERON; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN STABILITY;

ADENOSINE TRIPHOSPHATASES; AMINO ACID SEQUENCE; BACTERIAL PROTEINS; BASE SEQUENCE; DNA PRIMERS; ENDOPEPTIDASE CLP; GENES, BACTERIAL; GRAM-POSITIVE BACTERIA; HEAT-SHOCK PROTEINS; HYDROLYSIS; MOLECULAR SEQUENCE DATA; OPERON; PROTEIN KINASES; REPRESSOR PROTEINS; SEQUENCE DELETION; SEQUENCE HOMOLOGY, AMINO ACID; SERINE ENDOPEPTIDASES; TRANSCRIPTION, GENETIC;

BACILLUS SUBTILIS; ESCHERICHIA COLI; POSIBACTERIA;

EID: 0035865140     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/20.4.852     Document Type: Article

References (62)

1. Zinc fingers and other metal-binding domains. Elements for interaction between macromolecules
2. Dual channel imaging of two-dimensional electropherograms in Bacillus subtilis
3. The structures of Hs1U and the ATP-dependent protease Hs1U-Hs1V
4. Construction and characterization of new cloning vehicles II. A multipurpose cloning system
5. A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
6. The heat shock response in Escherichia coli
7. The ubiquitin-proteasome pathway: On protein death and cell life
8. CtsR, a novel regulator of stress and heat shock response, controls clp and molecular chaperone gene expression in Gram-positive bacteria
9. ClpE, a novel type of the HSP100 ATPase, is part of the CtsR heat shock regulon of Bacillus subtilis
10. The CtsR regulator of stress response is active as a dimer and specifically degraded in vivo at 37°C
11. Stress induction of the Bacillus subtilis clpP gene encoding the proteolytic component of the Clp protease and involvement of ClpP and ClpX in stress tolerance
12. Proteases and their targets in Escherichia coli
13. Regulatory subunits of energy-dependent proteases
14. Protein quality control: Triage by chaperones and proteases
15. The ClpXP and ClpAP proteases degrade proteins with carboxy-terminal peptide tails added by the SsrA tagging-system
16. B-regulon
17. Heat shock and general stress response in Bacillus subtilis
18. Genetic analysis in Bacillus subtilis
19. The role of the ClpA chaperone in proteolysis by ClpAP
20. Escherichia coli contains a soluble ATP-dependent protease (Ti) distinct from protease La
21. An essential protease involved in bacterial cell cycle control
22. Role of a peptide tagging system in degradation of proteins synthesized from damaged messenger RNA
23. Organization and regulation of an operon that encodes a sporulation-essential σ factor in Bacillus subtilis
24. Regulation of competence-specific gene expression by Mec-mediated protein-protein interaction in Bacillus subtilis
25. Catabolite repression of the Bacillus subitilis xyl operon involves a cis element functional in the context of an unrelated sequence and glucose exerts additional xylR-dependent repression
26. The first gene of the clpC-operon in Bacillus subtilis, ctsR, encodes a negative regulator of its own operon and other class III heat shock genes
27. Stress induction of clpC in Bacillus subtilis and its involvement in stress tolerance
28. Alternate promoters direct stress induced transcription of the Bacillus subtilis clpC operon
29. The Bacillus subtilis clpC operon encodes DNA repair and competence proteins
30. The Clp proteases of Bacillus subtilis are directly involved in degradation of misfolded proteins
31. Signal transduction network controlling degradative enzyme synthesis and competence in Bacillus subtilis
32. Cleavage of structural proteins during the assembly of the head of bacteriophage T4
33. Substrate targeting in the ubiquitin system
34. PDZ-like domains mediate binding specificity in the Clp/Hsp100 family of chaperones and protease regulatory subunits
35. Zinc fingers are sticking together
36. Heat shock response and protein degradation: Regulation of HSF2 by the ubiquitin-proteasome pathway
37. The GroE chaperone machine is a major modulator of the CIRCE heat shock regulon of Bacillus subtilis
38. Nonnative proteins induce expression of the Bacillus subtilis CIRCE regulon
39. Regulation of the heat shock transcription response: Cross talk between a family of heat shock factors, molecular chaperones and negative regulators
40. MecB of Bacillus subtilis, a member of the ClpC ATPase family, is a pleiotropic regulator controlling competence gene expression and survival at high temperature
41. ClpP of Bacillus subtilis is required for competence development, degradative enzyme synthesis, motility, growth at high temperature and sporulation
42. ClpE, a novel member of the Hsp100 family, is involved in cell division and virulence of Listeria monocytogens
43. CtsR controls class III heat shock gene expression in the human pathogen Listeria monocytogenes
44. H protein, in Bacillus subtilis at elevated temperatures
45. Concurrent chaperone and protease activities of ClpAP and requirement for the N-terminal ClpA ATP binding site for chaperone activity
46. Identification of a ClpC ATPase required for stress tolerance and in vivo survival of Listeria monocytogenes
47. The ClpC ATPase of Listeria monocytogenes is a general stress protein required for virulence and promoting of early bacterial escape from the phagosome of macrophages
48. HSP 100/Clp proteins: A common mechanism explains diverse functions
49. Genetics and physiology of the rel system of Bacillus subtilis
50. The Clp proteins - Proteolysis regulators or molecular chaperones
51. Use of T7 RNA polymerase to direct expression of cloned genes
52. Temporal activation of β-glucanase synthesis in Bacillus subtilis is mediated by the GTP pool
53. The N-end rule in bacteria
54. Nucleotide sequence of the Streptococcus faecalis plasmid gene encoding the 3′5″aminoglycoside phosphotransferase type III
55. Biochemical characterization of a molecular switch involving the heat shock protein ClpC, which controls the activity of ComK, the competence transcription factor of Bacillus subtilis
56. Competence in Bacillus subtilis is controlled by regulated proteolysis of a transcription factor
57. The N-end rule: Functions, mysteries, uses
58. Analysis of the induction of general stress proteins of Bacillus subtilis
59. Selectivity of intracellular proteolysis: Protein substrates activate the ATP-dependent protease (La)
60. Global-unfolding of a substrate protein by the Hspl00 chaperone ClpA
61. Posttranslational quality control: Folding, refolding and degrading proteins