期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 282, 期 14, 页码 10472-10479出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M611244200
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资金
- Biotechnology and Biological Sciences Research Council [BBS/E/C/00004150] Funding Source: researchfish
- Biotechnology and Biological Sciences Research Council [BBS/E/C/00004150] Funding Source: Medline
Sucrose nonfermenting-1 ( Snf1)-related protein kinase-1 ( SnRK1) of plants is a global regulator of carbon metabolism through the modulation of enzyme activity and gene expression. It is structurally and functionally related to the yeast protein kinase, Snf1, and to mammalian AMP-activated protein kinase. Two DNA sequences from Arabidopsis thaliana, previously known only by their data base accession numbers of NM_125448.3 ( protein ID NP_200863) and NM_114393.3 ( protein ID NP_ 566876) each functionally complemented a Saccharomyces cerevisiae elm1 sak1 tos3 triple mutant. This indicates that the Arabidopsis proteins are able to substitute for one of the missing yeast upstream kinases, which are required for activity of Snf1. Both plant proteins were shown to phosphorylate a peptide with the amino acid sequence of the phosphorylation site in the T-loop of SnRK1 and by inference SnRK1 in Arabidopsis. The proteins encoded by NM_125448.3 and NM_114393.3 have been named AtSnAK1 and AtSnAK2 ( Arabidopsis thaliana SnRK1-activating kinase), respectively. We believe this is the first time that upstream activators of SnRK1 have been described in any plant species.
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