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2-oxoglutarate modulates the affinity of FurA for the ntcA promoter in Anabaena sp. PCC 7120.
Guío, Jorge; Sarasa-Buisan, Cristina; Velázquez-Campoy, Adrián; Bes, María Teresa; Fillat, María F; Peleato, María Luisa; Sevilla, Emma.
Afiliação
  • Guío J; Departamento de Bioquímica y Biología Molecular y Celular, Institute for Biocomputation and Physics of Complex Systems, Universidad de Zaragoza, Spain.
  • Sarasa-Buisan C; Departamento de Bioquímica y Biología Molecular y Celular, Institute for Biocomputation and Physics of Complex Systems, Universidad de Zaragoza, Spain.
  • Velázquez-Campoy A; Departamento de Bioquímica y Biología Molecular y Celular, Institute for Biocomputation and Physics of Complex Systems, Universidad de Zaragoza, Spain.
  • Bes MT; Aragon Institute for Health Research (IIS Aragon), Zaragoza, Spain.
  • Fillat MF; Centro de Investigación Biomédica en Red en el Área Temática de Enfermedades Hepáticas y Digestivas (CIBERehd), Madrid, Spain.
  • Peleato ML; Fundacion ARAID, Government of Aragon, Zaragoza, Spain.
  • Sevilla E; Departamento de Bioquímica y Biología Molecular y Celular, Institute for Biocomputation and Physics of Complex Systems, Universidad de Zaragoza, Spain.
FEBS Lett ; 594(2): 278-289, 2020 01.
Article em En | MEDLINE | ID: mdl-31538336
ABSTRACT
2-oxoglutarate (2-OG) is a central metabolite that acts as a signaling molecule informing about the status of the carbon/nitrogen balance of the cell. In recent years, some transcriptional regulators and even two-component systems have been described as 2-OG sensors. In the nitrogen-fixing cyanobacterium Anabaena sp. PCC 7120, two master regulators, NtcA and FurA, are deeply involved in the regulation of nitrogen metabolism. Both of them show a complex intertwined regulatory circuit to achieve a suitable regulation of nitrogen fixation. In this work, 2-OG is found to bind FurA, modulating the specific binding of FurA to the ntcA promoter. This study provides evidence of a new additional control point in the complex network controlled by the NtcA and FurA proteins.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Proteínas de Bactérias / Fatores de Transcrição / Anabaena / Proteínas de Ligação a DNA / Ácidos Cetoglutáricos Idioma: En Revista: FEBS Lett Ano de publicação: 2020 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Proteínas de Bactérias / Fatores de Transcrição / Anabaena / Proteínas de Ligação a DNA / Ácidos Cetoglutáricos Idioma: En Revista: FEBS Lett Ano de publicação: 2020 Tipo de documento: Article