Unknown

Dataset Information

0

A novel transcription factor involved in plant defense endowed with protein phosphatase activity.


ABSTRACT: In plants, expression of a disease-resistance character following perception of a pathogen involves massive deployment of transcription-dependent defenses. Thus, if rapid and effective defense responses have to be achieved, it is crucial that the pathogenic signal is transduced and amplified through pre-existing signaling pathways. Reversible phosphorylation of specific transcription factors, by a concerted action of protein kinases and phosphatases, may represent a mechanism for rapid and flexible regulation of selective gene expression by environmental stimuli. Here we identified a novel DNA-binding protein from tobacco plants, designated DBP1, with protein phosphatase activity, which binds in a sequence-specific manner to a cis- acting element of a defense-related gene and participates in its transcriptional regulation. This finding helps delineate a terminal event in a signaling pathway for the selective activation of early transcription-dependent defense responses in plants, and suggests that stimulus-dependent reversible phosphorylation of regulatory proteins may occur directly in a transcription protein-DNA complex.

SUBMITTER: Carrasco JL 

PROVIDER: S-EPMC165647 | biostudies-literature | 2003 Jul

REPOSITORIES: biostudies-literature

altmetric image

Publications

A novel transcription factor involved in plant defense endowed with protein phosphatase activity.

Carrasco José L JL   Ancillo Gema G   Mayda Esther E   Vera Pablo P  

The EMBO journal 20030701 13


In plants, expression of a disease-resistance character following perception of a pathogen involves massive deployment of transcription-dependent defenses. Thus, if rapid and effective defense responses have to be achieved, it is crucial that the pathogenic signal is transduced and amplified through pre-existing signaling pathways. Reversible phosphorylation of specific transcription factors, by a concerted action of protein kinases and phosphatases, may represent a mechanism for rapid and flexi  ...[more]

Similar Datasets

| S-EPMC8666710 | biostudies-literature
| S-EPMC10759419 | biostudies-literature
| S-EPMC3942490 | biostudies-literature
| S-EPMC3044737 | biostudies-literature
| S-EPMC3655906 | biostudies-literature
| S-EPMC3793224 | biostudies-literature
| S-EPMC2572174 | biostudies-other
| S-EPMC7904156 | biostudies-literature
| S-EPMC10115308 | biostudies-literature
| S-EPMC9738932 | biostudies-literature