Plant Physiol. Journal of Pharmacology and Experimental Therapeutics
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Two SNF1-Related Protein Kinases from Spinach Leaf Phosphorylate and Inactivate 3-Hydroxy-3-Methylglutaryl-Coenzyme A Reductase, Nitrate Reductase, and Sucrose Phosphate Synthase in Vitro1

Christopher Sugden2, Paul G. Donaghy2, 3, Nigel G. Halford, and D. Grahame Hardie*

Biochemistry Department, Dundee University, Medical Sciences Institute/Wellcome Trust Building Complex, Dow Street, Dundee DD1 5EH, Scotland, United Kingdom (C.S., P.G.D., D.G.H.); and IACR-Long Ashton Research Station, Department of Agricultural Sciences, University of Bristol, Long Ashton, Bristol BS41 9AF, United Kingdom (N.G.H.)

We resolved from spinach (Spinacia oleracea) leaf extracts four Ca2+-independent protein kinase activities that phosphorylate the AMARAASAAALARRR (AMARA) and HMRSAMSGLHLVKRR (SAMS) peptides, originally designed as specific substrates for mammalian AMP-activated protein kinase and its yeast homolog, SNF1. The two major activities, HRK-A and HRK-C (3-hydroxy-3-methylglutaryl-coenzyme A reductase kinase A and C) were extensively purified and shown to be members of the plant SnRK1 (SNF1-related protein kinase 1) family using the following criteria: (a) They contain 58-kD polypeptides that cross-react with an antibody against a peptide sequence characteristic of the SnRK1 family; (b) they have similar native molecular masses and specificity for peptide substrates to mammalian AMP-activated protein kinase and the cauliflower homolog; (c) they are inactivated by homogeneous protein phosphatases and can be reactivated using the mammalian upstream kinase; and (d) they phosphorylate 3-hydroxy-3-methylglutaryl-coenzyme A reductase from Arabidopsis at the inactivating site, serine (Ser)-577. We propose that HRK-A and HRK-C represent either distinct SnRK1 isoforms or the same catalytic subunit complexed with different regulatory subunits. Both kinases also rapidly phosphorylate nitrate reductase purified from spinach, which is associated with inactivation of the enzyme that is observed only in the presence of 14-3-3 protein, a characteristic of phosphorylation at Ser-543. Both kinases also inactivate spinach sucrose phosphate synthase via phosphorylation at Ser-158. The SNF1-related kinases therefore potentially regulate several major biosynthetic pathways in plants: isoprenoid synthesis, sucrose synthesis, and nitrogen assimilation for the synthesis of amino acids and nucleotides.

1   This work was supported by a project grant from the Biotechnology and Biological Sciences Research Council (BBSRC) of the United Kingdom, by research studentships from the BBSRC to P.G.D. and C.S., and by grant-aided support from the BBSRC to IACR (N.G.H.).
2   These two authors contributed equally to the paper.
3   Present address: School of Biology and Biochemistry, Medical Biology Centre, The Queen's University of Belfast, Belfast BT9 7BL, Northern Ireland, UK.
*   Corresponding author; e-mail d.g.hardie{at}dundee.ac.uk; fax 44-1382-345-783.

Plant Physiol. (1999) 120: 257-274
Copyright Clearance Center:   0032-0889/99/120//18
© 1999 American Society of Plant Physiologists




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