Journal
ANNALS OF APPLIED BIOLOGY
Volume 153, Issue 3, Pages 401-409Publisher
WILEY-BLACKWELL
DOI: 10.1111/j.1744-7348.2008.00302.x
Keywords
AREBP; CDPK; metabolic signalling; SnRK1; SnRK2; SnRK3; stress
Categories
Funding
- Biotechnology and Biological Sciences Research Council of the UK
- Biotechnology and Biological Sciences Research Council [BBS/E/C/00004150] Funding Source: researchfish
- BBSRC [BBS/E/C/00004952] Funding Source: UKRI
Ask authors/readers for more resources
Evidence is provided that plant transcription factors of the ABA response element binding protein (AREBP) class are phosphorylated by sucrose non-fermenting-1-related protein kinase-1 (SnRK1) and a calcium-dependent protein kinase at highly conserved target sites. Two target sites for SnRK1 were identified in AREBPs using a specially developed motif search pipeline. Peptides containing the AREBP sites were phosphorylated by purified SnRK1 in vitro and by calcium-dependent and calcium-independent activities present in soluble protein extracted from Arabidopsis seedlings grown in liquid culture. Most (69-77%) of the calcium-independent phosphorylation of these peptides was removed by immunoprecipitation using anti-SnRK1 antisera, linking this activity unambiguously to SnRK1. It is possible that the protein kinase responsible for the calcium-dependent activity was SnRK3, a protein kinase that is related to SnRK1 and which has similar requirements for target site recognition. However, the involvement of other calcium-dependent protein kinases cannot be ruled out.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available