Repression of deoP2 in Escherichia coli by CytR: Conversion of a transcription activator into a repressor

EMBO Journal

Volumn 20, Issue 19, 2001, Pages 5392-5399

  Shin, Minsang ^a   Kang, Soim ^a   Hyun, Seok Jin ^a   Fujita, Nobuyuki ^b   Ishihama, Akira ^b   Valentin Hansen, Poul ^c   Choy, Hyon E ^a  

^a Chonnam National University Medical School   (South Korea)

^b NATIONAL INSTITUTE OF GENETICS   (Japan)

^c UNIVERSITY OF SOUTHERN DENMARK   (Denmark)

Author keywords

In vitro Dna protein interaction; Prokaryotic transcription initiation; Transcription activator; Transcription repressor

Indexed keywords

BACTERIAL PROTEIN; CYCLIC AMP; CYCLIC AMP BINDING PROTEIN; RNA POLYMERASE;

ARTICLE; CYTR GENE; DEOP2 GENE; ESCHERICHIA COLI; GENE; GENE REPRESSION; PRIORITY JOURNAL; PROMOTER REGION; PROTEIN DNA INTERACTION; TRANSCRIPTION INITIATION; TRANSCRIPTION REGULATION;

CARRIER PROTEINS; CYCLIC AMP RECEPTOR PROTEIN; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; GENE EXPRESSION REGULATION, BACTERIAL; MODELS, GENETIC; PROMOTER REGIONS (GENETICS); REPRESSOR PROTEINS; TRANS-ACTIVATORS;

EID: 0035476678     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/20.19.5392     Document Type: Article

References (57)

1. Interactions between the cyclic AMP receptor protein and the α subunit of RNA polymerase at the E. coli galP1 promoter
2. Mutations that alter the ability of Escherichia coli cyclic AMP receptor protein to activate transcription
3. Location of the C-terminal domain of the RNA polymerase α subunit in different open complexes at the E. coli galactose operon regulatory region
4. Transcription activation at promoters carrying tandem DNA sites for the Escherichia coli cyclic AMP receptor protein: Organisation of the RNA polymerase α subunits
5. Domain organization of RNA polymerase α subunit: C-terminal 85 amino acids constitute a domain capable of dimerization and DNA binding
6. Quantitative DNase I footprint titration; A method for studying protein-DNA interactions
7. Transcription activation at class II CAP-dependent promoters
8. Transcription activation by catabolite activator protein (CAP)
9. RNA polymerase idling and clearance in gal promoters: Use of supercoiled minicircle DNA template made in vivo
10. Repression and activation of transcription by Gal and Lac repressors: Involvement of α subunit of RNA polymerase
11. The -45 region of the Escherichia coli lac promoter: CAP-dependent and CAP-independent transcription
12. Activation of prokaryotic transcription through arbitrary protein-protein contacts
13. Escherichia coli catabolite gene activator protein mutants defective in positive control of lac operon transcription
14. Identification of an UP element consensus sequence for bacterial promoter
15. DNA-binding determinants of the α subunit of RNA polymerase: Novel DNA-binding domain architecture
16. Protein-protein contacts that activate and repress prokaryotic transcription
17. Bipartite functional map of the E. coli RNA polymerase α subunit: Involvement of the C-terminal region in transcription activation by cAMP-CRP
18. Protein-protein communication within the transcription apparatus
19. Flexible linker in the RNA polymerase α subunit facilitates the independent motion of the C-terminal activator contact domain
20. Design of CytR regulated, cAMP-CRP dependent class II promoters in Escherichia coli: RNA polymerase-promoter interactions modulate the efficiency of CytR repression
21. RNA polymerase α subunit binding site in positively controlled promoters: A new model for RNA polymerase-promoter interaction and transcriptional activation in the Escherichia coli ada and aidB genes
22. Spacing requirements for interactions between the C-terminal domain of the α subunit of Escherichia coli RNA polymerase and the cAMP receptor protein
23. Mechanism of CRP-cAMP activation of the lac operon: Transcription initiation activation of the P1 promoter
24. Dissection of a surface-exposed portion of the cAMP-CRP complex that mediates transcription activation and repression
25. Identification of the subunit of cAMP receptor protein (CRP) that functionally interacts with CytR in CRP-CytR-mediated transcriptional repression
26. The Escherichia coli RNA polymerase α subunit linker: Length requirements for transcription activation at CRP-dependent promoters
27. Characterization of promoter recognition complexes formed by CRP and CytR for repression and by CRP and RNA polymerase for activation of transcription on the Escherichia coli deoP2 promoter
28. Protein p4 represses phage φ29 A2c promoter by interacting with the α subunit of Bacillus subtilis RNA polymerase
29. Transcription factor recognition surface on the RNA polymerase α subunit is involved in contact with the DNA enhancer element
30. Positioning of two α subunit C-terminal domains of RNA polymerase at promoters by two transcription factors
31. Structural map of the α subunit of Escherichia coli RNA polymerase: Structural domains identified by proteolytic cleavage
32. Characterization of the activating region of Escherichia coli catabolite gene activator protein (CAP). Saturation and alanine-scanning mutagenesis
33. Transcription activation at class II CAP-dependent promoters: Two interactions between CAP and RNA polymerase
34. CAP, the -45 region and RNA polymerase: Three partners in transcription initiation at lacP1 in Escherichia coli
35. Transcription activation mediated by the C-terminal domain of the RNA polymerase α-subunit. Multipoint monitoring using a fluorescent probe
36. Transcriptional activation by recruitment
37. Factor independent activation of rrnB P1. An 'extended' promoter with an upstream element that dramatically increases promoter strength
38. Transcription activation at class II CRP-dependent promoters: The role of different activating regions
39. A third recognition element in bacterial promoters: DNA binding by the α subunit of RNA polymerase
40. Escherichia coli promoters with UP elements of different strengths: Modular structure of bacterial promoters
41. Reiterative transcription initiation from galP2 promoter of Escherichia coli
42. Transcription activation at Class II CRP-dependent promoters: Identification of determinants in the C-terminal domain of the RNA polymerase α subunit
43. Transcription activation at Escherichia coli promoters dependent on the cyclic AMP receptor protein: Effects of binding sequences for the RNA polymerase α-subunit
44. Protein-protein interactions in gene regulation: The cAMP-CRP complex sets the specificity of a second DNA-binding protein, the CytR repressor
45. The CytR repressor antagonizes cyclic AMP-cyclic AMP receptor protein activation of the deoCp2 promoter of Escherichia coli K-12
46. Tandem DNA-bound cAMP-CRP complexes are required for transcriptional repression of the deoP2 promoter by the CytR repressor in Escherichia coli
47. Single amino acid substitutions in the cAMP receptor protein specifically abolish regulation by the CytR repressor in Escherichia coli
48. A novel function of the cAMP-CRP complex in Escherichia coli: cAMP-CRP functions as an adaptor for the CytR repressor in the deo operon
49. An inactive open complex mediated by an UP element at Escherichia coli promoters
50. Location, structure and function of the target of a transcriptional activator protein
51. A flexible partnership: The CytR anti-activator and the cAMP-CRP activator protein, comrades in transcription control
52. Interactions between the Escherichia coli cyclic AMP receptor protein and RNA polymerase at class II promoters
53. The role of two surface exposed loops in transcription activation by the Escherichia coli CRP and FNR proteins
54. Orientation of functional activating regions in the E. coli CRP protein during transcription activation at class II promoters
55. The functional subunit of a dimeric transcription activator protein depends on promoter architecture
56. Identification of the activating region of catabolite gene activator protein (CAP): Isolation and characterization of mutants of CAP specifically defective in transcription activation
57. Identification of the functional subunit of a dimeric transcription activator protein by use of 'oriented heterodimers'