1H, 13C and 15N resonance assignments of σS activating protein Crl from Salmonella enterica serovar Typhimurium
Autor: | Christina Sizun, Françoise Norel, Paola Cavaliere |
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Přispěvatelé: | Systèmes macromoléculaires et Signalisation, Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS), Institut de Chimie des Substances Naturelles (ICSN), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), This work was supported by the French National Research Agency (Grant ANR-11-BSV3-009) and the IR-RMN-THC (CNRS FR3050), ANR-11-BSV3-0009,SIGMADAPT,Rôle de SigmaS dans la compétitivité et l'adaptation des bactéries à l'environnement(2011), Centre National de la Recherche Scientifique (CNRS)-Institut Pasteur [Paris], Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC), Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS), Centre National de la Recherche Scientifique (CNRS) |
Jazyk: | angličtina |
Rok vydání: | 2015 |
Předmět: |
Proton Magnetic Resonance Spectroscopy
Molecular Sequence Data Sigma factor MESH: Sequence Alignment MESH: Amino Acid Sequence Biology medicine.disease_cause Biochemistry Microbiology MESH: Proteus mirabilis/metabolism chemistry.chemical_compound Bacterial Proteins RpoS Structural Biology Transcription (biology) RNA polymerase MESH: Sigma Factor/metabolism medicine MESH: Carbon-13 Magnetic Resonance Spectroscopy Amino Acid Sequence Carbon-13 Magnetic Resonance Spectroscopy Proteus mirabilis Transcription factor Gene Escherichia coli MESH: Proton Magnetic Resonance Spectroscopy MESH: Molecular Sequence Data Nitrogen Isotopes Stress response fungi food and beverages MESH: Salmonella typhimurium/metabolism biology.organism_classification Cell biology Crl [SDV.MP]Life Sciences [q-bio]/Microbiology and Parasitology chemistry Salmonella enterica Salmonella Typhimurium Sequence Alignment rpoS MESH: Bacterial Proteins/chemistry MESH: Nitrogen Isotopes |
Zdroj: | Biomolecular NMR Assignments Biomolecular NMR Assignments, 2015, 9 (2), pp.397-401. ⟨10.1007/s12104-015-9617-z⟩ Biomolecular NMR Assignments, Springer, 2015, 9 (2), pp.397-401. ⟨10.1007/s12104-015-9617-z⟩ |
ISSN: | 1874-270X |
DOI: | 10.1007/s12104-015-9617-z⟩ |
Popis: | The general stress response in Enterobacteria, like Escherichia coli or Salmonella, is controlled by the transcription factor σS, encoded by the rpoS gene, which accumulates during stationary phase growth and associates with the core RNA polymerase enzyme (E) to promote transcription of genes involved in cell survival. Tight regulation of σS is essential to preserve the balance between self-preservation under stress conditions and nutritional competence in the absence of stress. Whereas σ factors are generally inactivated upon interaction with anti-sigma proteins, σS binding by the Crl protein facilitates the formation of the holoenzyme EσS, and therefore σS-controlled transcription. Previously, critical residues in both Crl and σS were identified and assigned to the binding interface in the Crl–σS complex. However, high-resolution structural data are missing to fully understand the molecular mechanisms underlying σS activation by Crl, in particular the possible role of Crl in triggering domain rearrangements in the multi-domain protein σS. Here we provide the 1H, 13C and 15N resonance assignments of Salmonella enterica serovar Typhimurium Crl, as a starting point for CrlSTM structure determination and further structural investigation of the CrlSTM–σ STM S complex. |
Databáze: | OpenAIRE |
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