Proline reduces the binding of transcriptional regulator ArgR to upstream of argB in Corynebacterium glutamicum.
Appl Microbiol Biotechnol
; 86(1): 235-42, 2010 Mar.
Article
en En
| MEDLINE
| ID: mdl-19798496
ABSTRACT
In this study, the ArgR-binding sites on the arg operon Corynbebacterium glutamicum were characterized by in vivo chromatin immunoprecipitation (ChIP). In addition, the ArgR-binding affinity in the presence of glutamate, proline, or arginine was examined to get further information on expression control. The ChIP assay showed that the ArgR protein binds specifically to the upstream regions of argC, argB, argF, and argG. Upon proline supplementation, ArgR-binding affinity was significantly reduced upstream of argB, resulting in increased ornithine production. In contrast, there was no change in the binding affinity of ArgR to the upstream regions of argC, argF, argG, or argB following the addition of glutamate and arginine. These results suggest that the upstream region of argB on the arg operon plays an important role in interacting with ArgR under proline-supplemented conditions and that proline causes an increase in the endogenous level of ornithine by reducing the binding affinity of ArgR to the upstream region of argB.
Texto completo:
1
Bases de datos:
MEDLINE
Asunto principal:
Proteínas Represoras
/
Proteínas Bacterianas
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Prolina
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Regulación Bacteriana de la Expresión Génica
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Corynebacterium glutamicum
Idioma:
En
Revista:
Appl Microbiol Biotechnol
Año:
2010
Tipo del documento:
Article
País de afiliación:
Corea del Sur