Access the full text.
Sign up today, get DeepDyve free for 14 days.
Nigel Halford, A. Man, J. Barker, W. Monger, P. Shewry, A. Smith, P. Purcell (1994)
Investigating the role of plant SNF1-related protein kinases.Biochemical Society transactions, 22 4
D. Carling, P. Clarke, V. Zammit, D. Hardie (1989)
Purification and characterization of the AMP-activated protein kinase. Copurification of acetyl-CoA carboxylase kinase and 3-hydroxy-3-methylglutaryl-CoA reductase kinase activities.European journal of biochemistry, 186 1-2
K. Ball, J. Barker, Nigel Halford, D. Hardie (1995)
Immunological evidence that HMG‐CoA reductase kinase‐A is the cauliflower homologue of the RKIN1 subfamily of plant protein kinasesFEBS Letters, 377
Tony Hunter (1994)
1001 protein kinases redux--towards 2000.Seminars in cell biology, 5 6
L Le Guen, M Thomas, M Bianchi, NG Halford, M Kreis (1992)
Structure and expression of a gene from Arabidopsis thalianaencoding a protein kinase related to the SNF1sub-family of protein kinasesGene, 120
M. Carlson, B. Osmond, L. Neigeborn, D. Botstein (1984)
A suppressor of SNF1 mutations causes constitutive high-level invertase synthesis in yeast.Genetics, 107 1
S. Davies, D. Carling, M. Munday, D. Hardie (1992)
Diurnal rhythm of phosphorylation of rat liver acetyl-CoA carboxylase by the AMP-activated protein kinase, demonstrated using freeze-clamping. Effects of high fat diets.European journal of biochemistry, 203 3
D. Carling, K. Aguan, A. Woods, A. Verhoeven, R. Beri, C. Brennan, C. Sidebottom, M. Davison, James Scott (1994)
Mammalian AMP-activated protein kinase is homologous to yeast and plant protein kinases involved in the regulation of carbon metabolism.The Journal of biological chemistry, 269 15
(1996)
Library screening with heterologous and homologous probes
(1992)
Transcriptional Regulators of Patatin Gene Expression
M. Munday, D. Campbell, D. Carling, D. Hardie (1988)
Identification by amino acid sequencing of three major regulatory phosphorylation sites on rat acetyl-CoA carboxylase.European journal of biochemistry, 175 2
Motoo Kimura (1983)
The neutral theory of molecular evolution.Scientific American, 241 5
S. Davies, D. Carling, D. Hardie (1989)
Tissue distribution of the AMP-activated protein kinase, and lack of activation by cyclic-AMP-dependent protein kinase, studied using a specific and sensitive peptide assay.European journal of biochemistry, 186 1-2
P. Sabelli, P. Shewry (1991)
Characterization and organization of gene families at the Gli-1 loci of bread and durum wheats by restriction fragment analysisTheoretical and Applied Genetics, 83
A. Woods, M. Munday, J. Scott, Xiaolu Yang, M. Carlson, D. Carling (1994)
Yeast SNF1 is functionally related to mammalian AMP-activated protein kinase and regulates acetyl-CoA carboxylase in vivo.The Journal of biological chemistry, 269 30
K. Ball, S. Dale, J. Weekes, D. Hardie (1994)
Biochemical characterization of two forms of 3-hydroxy-3-methylglutaryl-CoA reductase kinase from cauliflower (Brassica oleracia).European journal of biochemistry, 219 3
L. Guen, M. Thomas, M. Bianchi, Nigel Halford, M. Kreis (1992)
Structure and expression of a gene from Arabidopsis thaliana encoding a protein related to SNF1 protein kinase.Gene, 120 2
S. Davies, A. Sim, D. Hardie (1990)
Location and function of three sites phosphorylated on rat acetyl-CoA carboxylase by the AMP-activated protein kinase.European journal of biochemistry, 187 1
(1995)
The eukaryotic protein kinase superfamily
DG Hardie (1996)
Protein Phosphorylation in Plants
S. Hanks, A. Quinn, T. Hunter (1988)
The protein kinase family: conserved features and deduced phylogeny of the catalytic domains.Science, 241 4861
A. Sim, D. Hardie (1988)
The low activity of acetyl‐CoA car☐ylase in basal and glucagon‐stimulated hepatocytes is due to phosphorylation by the AMP‐activated protein kinase and not cyclic AMP‐dependent protein kinaseFEBS Letters, 233
J. Celenza, M. Carlson (1989)
Mutational analysis of the Saccharomyces cerevisiae SNF1 protein kinase and evidence for functional interaction with the SNF4 proteinMolecular and Cellular Biology, 9
J. Barker, S. Slocombe, K. Ball, D. Hardie, P. Shewry, Nigel Halford (1996)
Evidence That Barley 3-Hydroxy-3-Methylglutaryl-Coenzyme A Reductase Kinase Is a Member of the Sucrose Nonfermenting-1-Related Protein Kinase Family, 112
(1996)
The structure and function of the protein kinases: a survey
L. Neigeborn, M. Carlson (1984)
Genes affecting the regulation of SUC2 gene expression by glucose repression in Saccharomyces cerevisiae.Genetics, 108 4
Nigel Halford, J. Vicente-Carbajosa, P. Sabelli, P. Shewry, U. Hannappel, M. Kreis (1992)
Molecular analyses of a barley multigene family homologous to the yeast protein kinase gene SNF1.The Plant journal : for cell and molecular biology, 2 5
J. Gancedo (1992)
Carbon catabolite repression in yeast.European journal of biochemistry, 206 2
(1991)
Program Manual for the Wisconsin Package, Version 8, September 1994
M. Bradford (1976)
A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding.Analytical biochemistry, 72
Thomas Hardy, Dongqing Huang, P. Roach (1994)
Interactions between cAMP-dependent and SNF1 protein kinases in the control of glycogen accumulation in Saccharomyces cerevisiae.The Journal of biological chemistry, 269 45
J. Celenza, M. Carlson (1986)
A yeast gene that is essential for release from glucose repression encodes a protein kinase.Science, 233 4769
SK Hanks, T Hunter (1995)
The Protein Kinase Factsbook I
(1992)
from Arabidopsis thaliana encoding a protein kinase related to the SNF 1 sub - family of protein kinases
M. Holdsworth, C. Grierson, W. Schuch, M. Bevan (1992)
DNA-binding properties of cloned TATA-binding protein from potato tubersPlant Molecular Biology, 19
R. Mackintosh, S. Davies, P. Clarke, J. Weekes, J. Gillespie, Barry Gibb, D. Hardie (1992)
Evidence for a protein kinase cascade in higher plants. 3-Hydroxy-3-methylglutaryl-CoA reductase kinase.European journal of biochemistry, 209 3
J. Logemann, Jeff Schell, Lothar Willmitzer (1987)
Improved method for the isolation of RNA from plant tissues.Analytical biochemistry, 163 1
U. Hannappel, J. Vicente-Carbajosa, J. Barker, P. Shewry, Nigel Halford (1995)
Differential expression of two barley SNF1-related protein kinase genesPlant Molecular Biology, 27
Toshiya Muranaka, H. Banno, Yasunori Machida (1994)
Characterization of tobacco protein kinase NPK5, a homolog of Saccharomyces cerevisiae SNF1 that constitutively activates expression of the glucose-repressible SUC2 gene for a secreted invertase of S. cerevisiaeMolecular and Cellular Biology, 14
A. Alderson, P. Sabelli, J. Dickinson, D. Cole, M. Richardson, M. Kreis, P. Shewry, Nigel Halford (1991)
Complementation of snf1, a mutation affecting global regulation of carbon metabolism in yeast, by a plant protein kinase cDNA.Proceedings of the National Academy of Sciences of the United States of America, 88 19
RW Mackintosh, SP Davies, PR Clarke, J Weekes, JG Gillespie, BJ Gibb, DG Hardie (1992)
Evidence for a protein kinase cascade in higher plantsEur J Biochem, 209
P. Clarke, D. Hardie (1990)
Regulation of HMG‐CoA reductase: identification of the site phosphorylated by the AMP‐activated protein kinase in vitro and in intact rat liver.The EMBO Journal, 9
S. Thompson-Jaeger, Jean Francois, P. Gaughran, K. Tatchell (1991)
Deletion of SNF1 affects the nutrient response of yeast and resembles mutations which activate the adenylate cyclase pathway.Genetics, 129 3
M. Carlson, B. Osmond, D. Botstein (1981)
Mutants of yeast defective in sucrose utilization.Genetics, 98 1
NG Halford (1996)
Plant Gene Isolation
A polymerase chain reaction product (PKIN503) was amplified from potato (Solanum tuberosum) cv. Désirée using oligonucleotide primers with sequences which are highly conserved in the plant sucrose non-fermenting 1 (SNF1)-related protein kinase gene family. Southern blot analysis showed the presence of 5–10 SNF1-related genes in the potato genome. PKIN503 was used to screen a tuber cDNA library and a genomic library, and one cDNA and five genomic clones were isolated. The nucleotide sequences of a portion of all five genomic clones were shown to be identical and only one, pgPKIN1, was analysed further. The cDNA was found to be truncated at the 5′ end but the cDNA and genomic sequences contained only 15 substitutions, two of which resulted in changes in the derived amino acid sequence. PKIN1 was shown to encode an Mr 57854 protein with 61–70% sequence similarity with other plant SNF1-related protein kinases. Northern blot analysis revealed some tissue-specific differences in PKIN1 transcript levels, the lowest being detected in leaves and the highest in stolons. However, much greater differences were found in SNF1-related activity, which was measured using a phosphorylation assay with a substrate peptide which has been shown previously to be phosphorylated by plant SNF1-related protein kinases. Activity decreased by almost 80% during development from stolons to mature tubers but it increased about seven-fold during the first seven days of storage after harvesting, before decreasing again. However, activity was highest in mini-tubers, where the levels were 37 times greater than those in mature tubers from a pot-grown plant. Transcript levels in these tissues were approximately equal, clear evidence that SNF1-related protein kinase activity in potato is regulated, in part, post-transcriptionally.
Plant Molecular Biology – Springer Journals
Published: Sep 29, 2004
Read and print from thousands of top scholarly journals.
Already have an account? Log in
Bookmark this article. You can see your Bookmarks on your DeepDyve Library.
To save an article, log in first, or sign up for a DeepDyve account if you don’t already have one.
Copy and paste the desired citation format or use the link below to download a file formatted for EndNote
Access the full text.
Sign up today, get DeepDyve free for 14 days.
All DeepDyve websites use cookies to improve your online experience. They were placed on your computer when you launched this website. You can change your cookie settings through your browser.