The assimilation of gamma-butyrolactone in Agrobacterium tumefaciens C58 interferes with the accumulation of the N-acyl-homoserine lactone signal.
Mol Plant Microbe Interact
; 17(9): 951-7, 2004 Sep.
Article
en En
| MEDLINE
| ID: mdl-15384485
Agrobacterium tumefaciens C58 communicates using N-acyl-homoserine lactones (acyl-HSL) and contains two lactonase-encoding genes, attM and aiiB, the products of which are capable of inactivating the acyl-HSL signal. In A. tumefaciens A6, the expression of the attKLM operon is controlled by the transcriptional repressor encoded by an adjacent gene, attJ. An attJ::Tn5 mutant does not accumulate acyl-HSL because of the constitutive expression of the lactonase AttM, the activity of which inactivates acyl-HSL. In this work, the attKLM operon of A. tumefaciens C58 was shown to be involved in an assimilative pathway of gamma-butyrolactone (GBL), gamma-hydroxybutyrate (GHB), and succinate semialdehyde (SSA), in which AttM and AttL are key enzymes for GBL and GHB assimilation. The expression of the attKLM promoter was activated in the presence of GBL, GHB, and SSA. Under these conditions, A. tumefaciens C58 did not accumulate the acyl-HSL that it naturally synthesizes, and also became able to inactivate exogenous acyl-HSL signals. Therefore, in A. tumefaciens C58, the assimilative pathway of gamma-butyrolactone interferes with the acyl-HSL signaling.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
4-Butirolactona
/
Agrobacterium tumefaciens
Idioma:
En
Revista:
Mol Plant Microbe Interact
Asunto de la revista:
BIOLOGIA MOLECULAR
/
BOTANICA
/
MICROBIOLOGIA
Año:
2004
Tipo del documento:
Article
País de afiliación:
Francia
Pais de publicación:
Estados Unidos