Inter-domain cross-talk controls the NifA protein activity of Herbaspirillum seropedicae.
FEBS Lett
; 508(1): 1-4, 2001 Nov 09.
Article
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| MEDLINE
| ID: mdl-11707257
ABSTRACT
Herbaspirillum seropedicae is an endophytic diazotroph, which colonizes sugar cane, wheat, rice and maize. The activity of NifA, a transcriptional activator of nif genes in H. seropedicae, is controlled by ammonium ions through a mechanism involving its N-terminal domain. Here we show that this domain interacts specifically in vitro with the N-truncated NifA protein, as revealed by protection against proteolysis, and this interaction caused an inhibitory effect on both the ATPase and DNA-binding activities of the N-truncated NifA protein. We suggest that the N-terminal domain inhibits NifA-dependent transcriptional activation by an inter-domain cross-talk between the catalytic domain of the NifA protein and its regulatory N-terminal domain in response to fixed nitrogen.
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Base de datos:
MEDLINE
Asunto principal:
Proteínas Bacterianas
/
Factores de Transcripción
/
Betaproteobacteria
Idioma:
En
Revista:
FEBS Lett
Año:
2001
Tipo del documento:
Article
País de afiliación:
Brasil