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Proceedings of the National Academy of Sciences - PNAS, 2006-02, Vol.103 (6), p.1988-1993
2006
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Autor(en) / Beteiligte
Titel
Abscisic acid-dependent multisite phosphorylation regulates the activity of a transcription activator AREB1
Ist Teil von
  • Proceedings of the National Academy of Sciences - PNAS, 2006-02, Vol.103 (6), p.1988-1993
Ort / Verlag
United States: National Academy of Sciences
Erscheinungsjahr
2006
Quelle
MEDLINE
Beschreibungen/Notizen
  • bZIP-type transcription factors AREBs/ABFs bind an abscisic acid (ABA)-responsive cis-acting element named ABRE and transactivate downstream gene expression in Arabidopsis. Because AREB1 overexpression could not induce downstream gene expression, activation of AREB1 requires ABA-dependent posttranscriptional modification. We confirmed that ABA activated 42-kDa kinase activity, which, in turn, phosphorylated Ser/Thr residues of R-X-X-S/T sites in the conserved regions of AREB1. Amino acid substitutions of R-X-X-S/T sites to Ala suppressed transactivation activity, and multiple substitution of these sites resulted in almost complete suppression of transactivation activity in transient assays. In contrast, substitution of the Ser/Thr residues to Asp resulted in high transactivation activity without exogenous ABA application. A phosphorylated, transcriptionally active form was achieved by substitution of Ser/Thr in all conserved R-X-X-S/T sites to Asp. Transgenic plants overexpressing the phosphorylated active form of AREB1 expressed many ABA-inducible genes, such as RD29B, without ABA treatment. These results indicate that the ABA-dependent multisite phosphorylation of AREB1 regulates its own activation in plants.
Sprache
Englisch
Identifikatoren
ISSN: 0027-8424
eISSN: 1091-6490
DOI: 10.1073/pnas.0505667103
Titel-ID: cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_1413621

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