Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2003-11-12
pubmed:abstractText
In plants, excess cellular lysine (Lys) is catabolized into glutamic acid and acetyl-coenzyme A; yet, it is still not clear whether this pathway has other functions in addition to balancing Lys levels. To address this issue, we examined the effects of stress-related hormones, abscisic acid (ABA), and jasmonate, as well as various metabolic signals on the production of the mRNA and polypeptide of the bifunctional Lys-ketoglutarate reductase (LKR)/saccharopine dehydrogenase (SDH) enzyme, which contains the first two linked enzymes of Lys catabolism. The level of LKR/SDH was strongly enhanced by ABA, jasmonate, and sugar starvation, whereas excess sugars and nitrogen starvation reduced its level; thus this pathway appears to fulfill multiple functions in stress-related and carbon/nitrogen metabolism. Treatments with combination of hormones and/or metabolites, as well as use of ABA mutants in conjunction with the tester sugars mannose and 3-O-methyl-glucose further supported the idea that the hormonal and metabolic signals apparently operate through different signal transduction cascades. The stimulation of LKR/SDH protein expression by ABA is regulated by a signal transduction cascade that contains the ABI1-1 and ABI2-1 protein phosphatases. By contrast, the stimulation of LKR/SDH protein expression by sugar starvation is regulated by the hexokinase-signaling cascade in a similar manner to the repression of many photosynthetic genes by sugars. These findings suggest a metabolic and mechanistic link between Lys catabolism and photosynthesis-related metabolism in the regulation of carbon/nitrogen partitioning.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/14576281-10908876, http://linkedlifedata.com/resource/pubmed/commentcorrection/14576281-11312138, http://linkedlifedata.com/resource/pubmed/commentcorrection/14576281-11343924, http://linkedlifedata.com/resource/pubmed/commentcorrection/14576281-11500552, http://linkedlifedata.com/resource/pubmed/commentcorrection/14576281-11912238, http://linkedlifedata.com/resource/pubmed/commentcorrection/14576281-12045268, http://linkedlifedata.com/resource/pubmed/commentcorrection/14576281-12045275, http://linkedlifedata.com/resource/pubmed/commentcorrection/14576281-12045277, http://linkedlifedata.com/resource/pubmed/commentcorrection/14576281-12087111, http://linkedlifedata.com/resource/pubmed/commentcorrection/14576281-5432063, http://linkedlifedata.com/resource/pubmed/commentcorrection/14576281-7640525, http://linkedlifedata.com/resource/pubmed/commentcorrection/14576281-8146157, http://linkedlifedata.com/resource/pubmed/commentcorrection/14576281-8535146, http://linkedlifedata.com/resource/pubmed/commentcorrection/14576281-9286108, http://linkedlifedata.com/resource/pubmed/commentcorrection/14576281-942051, http://linkedlifedata.com/resource/pubmed/commentcorrection/14576281-9634796
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/ABI1 protein, Arabidopsis, http://linkedlifedata.com/resource/pubmed/chemical/ABI2 protein, Arabidopsis, http://linkedlifedata.com/resource/pubmed/chemical/Abscisic Acid, http://linkedlifedata.com/resource/pubmed/chemical/Arabidopsis Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Carbohydrates, http://linkedlifedata.com/resource/pubmed/chemical/Cyclopentanes, http://linkedlifedata.com/resource/pubmed/chemical/Hexokinase, http://linkedlifedata.com/resource/pubmed/chemical/Lysine, http://linkedlifedata.com/resource/pubmed/chemical/Nitrogen, http://linkedlifedata.com/resource/pubmed/chemical/Oxylipins, http://linkedlifedata.com/resource/pubmed/chemical/Phosphates, http://linkedlifedata.com/resource/pubmed/chemical/Phosphoprotein Phosphatases, http://linkedlifedata.com/resource/pubmed/chemical/Saccharopine Dehydrogenases, http://linkedlifedata.com/resource/pubmed/chemical/jasmonic acid, http://linkedlifedata.com/resource/pubmed/chemical/saccharopine dehydrogenase (NADP ...
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0032-0889
pubmed:author
pubmed:issnType
Print
pubmed:volume
133
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1407-15
pubmed:dateRevised
2010-9-20
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
Synthesis of the Arabidopsis bifunctional lysine-ketoglutarate reductase/saccharopine dehydrogenase enzyme of lysine catabolism is concertedly regulated by metabolic and stress-associated signals.
pubmed:affiliation
Department of Plant Sciences, The Weizmann Institute of Science, Rehovot 76100 Israel.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't