Arabidopsis sucrose non-fermenting-1-related protein kinase-1 and calcium-dependent protein kinase phosphorylate conserved target sites in ABA response element binding proteins

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https://doi.org/10.1111/j.1744-7348.2008.00302.x
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Keywords

AREBP, CDPK, Metabolic signalling, SnRK1, SnRK2, SnRK3, Stress

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Arabidopsis sucrose non-fermenting-1-related protein kinase-1 and calcium-dependent protein kinase phosphorylate conserved target sites in ABA response element binding proteins. / Zhang, Y.; Andralojc, P. J.; Hey, S. J. et al.
In: Annals of Applied Biology, Vol. 153, No. 3, 01.12.2008, p. 401-409.

Research output: Contribution to Journal/Magazine › Journal article › peer-review

Bibtex

@article{dd5b8e0127a24b5fbf1ea14018e4a497,

title = "Arabidopsis sucrose non-fermenting-1-related protein kinase-1 and calcium-dependent protein kinase phosphorylate conserved target sites in ABA response element binding proteins",

abstract = "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.",

keywords = "AREBP, CDPK, Metabolic signalling, SnRK1, SnRK2, SnRK3, Stress",

author = "Y. Zhang and Andralojc, {P. J.} and Hey, {S. J.} and Primavesi, {L. F.} and M. Specht and J. Koehler and Parry, {M. A J} and Halford, {N. G.}",

year = "2008",

month = dec,

day = "1",

doi = "10.1111/j.1744-7348.2008.00302.x",

language = "English",

volume = "153",

pages = "401--409",

journal = "Annals of Applied Biology",

issn = "0003-4746",

publisher = "Wiley-Blackwell",

number = "3",

}

RIS

TY - JOUR

T1 - Arabidopsis sucrose non-fermenting-1-related protein kinase-1 and calcium-dependent protein kinase phosphorylate conserved target sites in ABA response element binding proteins

AU - Zhang, Y.

AU - Andralojc, P. J.

AU - Hey, S. J.

AU - Primavesi, L. F.

AU - Specht, M.

AU - Koehler, J.

AU - Parry, M. A J

AU - Halford, N. G.

PY - 2008/12/1

Y1 - 2008/12/1

N2 - 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.

AB - 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.

KW - AREBP

KW - CDPK

KW - Metabolic signalling

KW - SnRK1

KW - SnRK2

KW - SnRK3

KW - Stress

UR - http://www.scopus.com/inward/record.url?scp=57349180847&partnerID=8YFLogxK

U2 - 10.1111/j.1744-7348.2008.00302.x

DO - 10.1111/j.1744-7348.2008.00302.x

M3 - Journal article

AN - SCOPUS:57349180847

VL - 153

SP - 401

EP - 409

JO - Annals of Applied Biology

JF - Annals of Applied Biology

SN - 0003-4746

IS - 3

ER -

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