Difference between revisions of "Transcription antiterminators"
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| − | ==Transcription antiterminators controlled by PTS-dependent phosphorylation== | + | ==Transcription antiterminators controlled by [[PTS]]-dependent phosphorylation== |
| − | These proteins exert positive control of gene expression by transcription antitermination. They regulate the uptake and utilization of specific sugars that are transported by the phosphotransferase system (PTS). | + | These proteins exert positive control of gene expression by transcription antitermination. They regulate the uptake and utilization of specific sugars that are transported by the phosphotransferase system ([[PTS]]). |
| − | Their activity is negatively regulated in the absence of the specific inducer by phosphorylation by the corresponding Enzyme II of the PTS. This results in their inactivity. In the presence of the inducer, the phosphate group is drained to the transported substrate and the active regulators lead to expression of their corresponding catabolic operons. | + | Their activity is negatively regulated in the absence of the specific inducer by phosphorylation by the corresponding Enzyme II of the [[PTS]]. This results in their inactivity. In the presence of the inducer, the phosphate group is drained to the transported substrate and the active regulators lead to expression of their corresponding catabolic operons. |
In addition, many PRD-containing regulators are positively controlled by [[PtsH|HPr]]-dependent phosphorylation. This phosphorylation occurs in the absence of glucose and other preferred carbon sources and is part of catabolite repression. | In addition, many PRD-containing regulators are positively controlled by [[PtsH|HPr]]-dependent phosphorylation. This phosphorylation occurs in the absence of glucose and other preferred carbon sources and is part of catabolite repression. | ||
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* [[SacT]]: allows expression of the ''[[sacP]]-[[sacA]]'' operon in the presence of sucrose | * [[SacT]]: allows expression of the ''[[sacP]]-[[sacA]]'' operon in the presence of sucrose | ||
* [[SacY]]: allows expression of the ''[[sacX]]-[[sacY]]'' operon and the ''[[sacB]]'' gene in the presence of sucrose | * [[SacY]]: allows expression of the ''[[sacX]]-[[sacY]]'' operon and the ''[[sacB]]'' gene in the presence of sucrose | ||
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==Transcription antiterminators controlled by low molecular weight effectors== | ==Transcription antiterminators controlled by low molecular weight effectors== | ||
Latest revision as of 13:58, 5 December 2011
Transcription antiterminators controlled by PTS-dependent phosphorylation
These proteins exert positive control of gene expression by transcription antitermination. They regulate the uptake and utilization of specific sugars that are transported by the phosphotransferase system (PTS). Their activity is negatively regulated in the absence of the specific inducer by phosphorylation by the corresponding Enzyme II of the PTS. This results in their inactivity. In the presence of the inducer, the phosphate group is drained to the transported substrate and the active regulators lead to expression of their corresponding catabolic operons. In addition, many PRD-containing regulators are positively controlled by HPr-dependent phosphorylation. This phosphorylation occurs in the absence of glucose and other preferred carbon sources and is part of catabolite repression.
- GlcT: allows expression of the ptsG-ptsH-ptsI operon in the presence of glucose
- LicT: allows expression of the bglS gene and the bglP-bglH operon in the presence of ß-glucosides
- SacT: allows expression of the sacP-sacA operon in the presence of sucrose
- SacY: allows expression of the sacX-sacY operon and the sacB gene in the presence of sucrose
Transcription antiterminators controlled by low molecular weight effectors
Reviews
Jörg Stülke
Control of transcription termination in bacteria by RNA-binding proteins that modulate RNA structures.
Arch Microbiol: 2002, 177(6);433-40
[PubMed:12029388]
[WorldCat.org]
[DOI]
(P p)
H van Tilbeurgh, N Declerck
Structural insights into the regulation of bacterial signalling proteins containing PRDs.
Curr Opin Struct Biol: 2001, 11(6);685-93
[PubMed:11751049]
[WorldCat.org]
[DOI]
(P p)
J Stülke, M Arnaud, G Rapoport, I Martin-Verstraete
PRD--a protein domain involved in PTS-dependent induction and carbon catabolite repression of catabolic operons in bacteria.
Mol Microbiol: 1998, 28(5);865-74
[PubMed:9663674]
[WorldCat.org]
[DOI]
(P p)
B Rutberg
Antitermination of transcription of catabolic operons.
Mol Microbiol: 1997, 23(3);413-21
[PubMed:9044276]
[WorldCat.org]
[DOI]
(P p)
