Effect of ATP and 2-oxoglutarate on the in vitro interaction between the NifA GAF domain and the GlnB protein of Azospirillum brasilense
Braz. j. med. biol. res
; 45(12): 1135-1140, Dec. 2012. ilus, tab
Artículo
en Inglés
| LILACS
| ID: lil-659653
Biblioteca responsable:
BR1.1
ABSTRACT
Azospirillum brasilense is a diazotroph that associates with important agricultural crops and thus has potential to be a nitrogen biofertilizer. The A. brasilense transcription regulator NifA, which seems to be constitutively expressed, activates the transcription of nitrogen fixation genes. It has been suggested that the nitrogen status-signaling protein GlnB regulates NifA activity by direct interaction with the NifA N-terminal GAF domain, preventing the inhibitory effect of this domain under conditions of nitrogen fixation. In the present study, we show that an N-terminal truncated form of NifA no longer required GlnB for activity and lost regulation by ammonium. On the other hand, in trans co-expression of the N-terminal GAF domain inhibited the N-truncated protein in response to fixed nitrogen levels. We also used pull-down assays to show in vitro interaction between the purified N-terminal GAF domain of NifA and the GlnB protein. The results showed that A. brasilense GlnB interacts directly with the NifA N-terminal domain and this interaction is dependent on the presence of ATP and 2-oxoglutarate.
Texto completo:
Disponible
Colección:
Bases de datos internacionales
Base de datos:
LILACS
Asunto principal:
Proteínas Bacterianas
/
Factores de Transcripción
/
Azospirillum brasilense
/
Adenosina Trifosfato
/
Beta-Galactosidasa
/
Ácidos Cetoglutáricos
País/Región como asunto:
America del Sur
/
Brasil
Idioma:
Inglés
Revista:
Braz. j. med. biol. res
Asunto de la revista:
Biologia
/
Medicina
Año:
2012
Tipo del documento:
Artículo
País de afiliación:
Brasil
Institución/País de afiliación:
Universidade Federal do Paraná/BR
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