Light affects salt stress-induced transcriptional memory of P5CS1 in Arabidopsis.
Proc Natl Acad Sci U S A
; 113(51): E8335-E8343, 2016 12 20.
Article
en En
| MEDLINE
| ID: mdl-27930298
To cope with environmental stresses, plants often adopt a memory response upon primary stress exposure to facilitate a quicker and stronger reaction to recurring stresses. However, it remains unknown whether light is involved in the manifestation of stress memory. Proline accumulation is a striking metabolic adaptation of higher plants during various environmental stresses. Here we show that salinity-induced proline accumulation is memorable and HY5-dependent light signaling is required for such a memory response. Primary salt stress induced the expression of Δ1-pyrroline-5-carboxylate synthetase 1 (P5CS1), encoding a proline biosynthetic enzyme and proline accumulation, which were reduced to basal level during the recovery stage. Reoccurring salt stress-induced stronger P5CS1 expression and proline accumulation were dependent upon light exposure during the recovery stage. Further studies demonstrated that salt-induced transcriptional memory of P5CS1 is associated with the retention of increased H3K4me3 level at P5CS1 during the recovery stage. HY5 binds directly to light-responsive element, C/A-box, in the P5CS1 promoter. Deletion of the C/A-box or hy5 hyh mutations caused rapid reduction of H3K4me3 level at P5CS1 during the recovery stage, resulting in impairment of the stress memory response. These results unveil a previously unrecognized mechanism whereby light regulates salt-induced transcriptional memory via the function of HY5 in maintaining H3K4me3 level at the memory gene.
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Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Sales (Química)
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Estrés Fisiológico
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Proteínas Nucleares
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Arabidopsis
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Fosfotransferasas (Aceptor de Grupo Alcohol)
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Proteínas de Arabidopsis
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Glutamato-5-Semialdehído Deshidrogenasa
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Factores de Transcripción con Cremalleras de Leucina de Carácter Básico
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Luz
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Complejos Multienzimáticos
Idioma:
En
Revista:
Proc Natl Acad Sci U S A
Año:
2016
Tipo del documento:
Article
País de afiliación:
China
Pais de publicación:
Estados Unidos