Transcription regulators controlled by interaction with enzyme IIB components of the phosphoenolpyruvate:sugar phosphotransferase system

Autor: Eliane Milohanic, Francine Moussan Désirée Aké, Meriem Derkaoui, Houda Bouraoui, Arthur Constant Zébré, Thanh Nguyen Cao, Josef Deutscher, Sylvie Nessler, Philippe Joyet, Magali Ventroux, Marie-Françoise Noirot-Gros
Přispěvatelé: MICrobiologie de l'ALImentation au Service de la Santé (MICALIS), Institut National de la Recherche Agronomique (INRA)-AgroParisTech, Institut de biochimie et biophysique moléculaire et cellulaire (IBBMC), Université Paris-Sud - Paris 11 (UP11)-Centre National de la Recherche Scientifique (CNRS), Agence National de la Recherche [ANR-09-BLANC-0273-01]
Jazyk: angličtina
Rok vydání: 2013
Předmět:
LACTOBACILLUS-CASEI
[SDV.SA]Life Sciences [q-bio]/Agricultural sciences
Operon
Biophysics
Repressor
macromolecular substances
Biology
Biochemistry
PTS inhibition
Analytical Chemistry
BACILLUS-SUBTILIS
03 medical and health sciences
Bacterial Proteins
Transcription (biology)
CARBON CATABOLITE REPRESSION
Transcriptional regulation
CRYSTAL-STRUCTURE
MULTIPLE PHOSPHORYLATION
Phosphorylation
Phosphoenolpyruvate Sugar Phosphotransferase System
PTS regulation domain
LISTERIA-MONOCYTOGENES
Molecular Biology
030304 developmental biology
0303 health sciences
Binding Sites
Models
Genetic
030306 microbiology
Kinase
Activator (genetics)
Escherichia coli Proteins
INDUCER EXCLUSION
Gene Expression Regulation
Bacterial
PEP group translocation
Transcription regulation
Repressor Proteins
CATALYZED PHOSPHORYLATION
ESCHERICHIA-COLI
Membrane sequestration
Phosphoenolpyruvate:sugar phosphotransferase system
VIRULENCE GENE REPRESSION
Trans-Activators
bacteria
Protein Binding
Zdroj: Biochimica et Biophysica Acta Proteins and Proteomics
Biochimica et Biophysica Acta Proteins and Proteomics, Elsevier, 2013, 1834 (7), pp.1415-1424. ⟨10.1016/j.bbapap.2013.01.004⟩
ISSN: 1570-9639
DOI: 10.1016/j.bbapap.2013.01.004⟩
Popis: Numerous bacteria possess transcription activators and antiterminators composed of regulatory domains phosphorylated by components of the phosphoenolpyruvate:sugar phosphotransferase system (PTS). These domains, called PTS regulation domains (PRDs), usually contain two conserved histidines as potential phosphorylation sites. While antiterminators possess two PRDs with four phosphorylation sites, transcription activators contain two PRDs plus two regulatory domains resembling PTS components (EIIA and EIIB). The activity of these transcription regulators is controlled by up to five phosphorylations catalyzed by PTS proteins. Phosphorylation by the general PTS components El and HPr is usually essential for the activity of PRD-containing transcription regulators, whereas phosphorylation by the sugar-specific components ERA or EIIB lowers their activity. For a specific regulator, for example the Bacillus subtilis mtl operon activator MtIR, the functional phosphorylation sites can be different in other bacteria and consequently the detailed mode of regulation varies. Some of these transcription regulators are also controlled by an interaction with a sugar-specific EIIB PTS component. The EIIBs are frequently fused to the membrane-spanning EIIC and EIIB-mediated membrane sequestration is sometimes crucial for the control of a transcription regulator. This is also true for the Escherichia coli repressor Mlc, which does not contain a PRD but nevertheless interacts with the EIIB domain of the glucose-specific PTS. In addition, some PRD-containing transcription activators interact with a distinct EIIB protein located in the cytoplasm. The phosphorylation state of the EIIB components, which changes in response to the presence or absence of the corresponding carbon source, affects their interaction with transcription regulators. This article is part of a Special Issue entitled: Inhibitors of Protein Kinases (2012). (C) 2013 Elsevier B.V. All rights reserved.
Databáze: OpenAIRE
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