Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1998-4-16
pubmed:abstractText
The tryptophan (Trp) biosynthetic pathway leads to the production of many secondary metabolites with diverse functions, and its regulation is predicted to respond to the needs for both protein synthesis and secondary metabolism. We have tested the response of the Trp pathway enzymes and three other amino acid biosynthetic enzymes to starvation for aromatic amino acids, branched-chain amino acids, or methionine. The Trp pathway enzymes and cytosolic glutamine synthetase were induced under all of the amino acid starvation test conditions, whereas methionine synthase and acetolactate synthase were not. The mRNAs for two stress-inducible enzymes unrelated to amino acid biosynthesis and accumulation of the indolic phytoalexin camalexin were also induced by amino acid starvation. These results suggest that regulation of the Trp pathway enzymes under amino acid deprivation conditions is largely a stress response to allow for increased biosynthesis of secondary metabolites. Consistent with this hypothesis, treatments with the oxidative stress-inducing herbicide acifluorfen and the abiotic elicitor alpha-amino butyric acid induced responses similar to those induced by the amino acid starvation treatments. The role of salicylic acid in herbicide-mediated Trp and camalexin induction was investigated.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/9501110-11607524, http://linkedlifedata.com/resource/pubmed/commentcorrection/9501110-11607545, http://linkedlifedata.com/resource/pubmed/commentcorrection/9501110-11607555, http://linkedlifedata.com/resource/pubmed/commentcorrection/9501110-1392589, http://linkedlifedata.com/resource/pubmed/commentcorrection/9501110-1392592, http://linkedlifedata.com/resource/pubmed/commentcorrection/9501110-16594071, http://linkedlifedata.com/resource/pubmed/commentcorrection/9501110-16653032, http://linkedlifedata.com/resource/pubmed/commentcorrection/9501110-16666004, http://linkedlifedata.com/resource/pubmed/commentcorrection/9501110-16668708, http://linkedlifedata.com/resource/pubmed/commentcorrection/9501110-1681544, http://linkedlifedata.com/resource/pubmed/commentcorrection/9501110-1684022, http://linkedlifedata.com/resource/pubmed/commentcorrection/9501110-17810266, http://linkedlifedata.com/resource/pubmed/commentcorrection/9501110-1820820, http://linkedlifedata.com/resource/pubmed/commentcorrection/9501110-2351688, http://linkedlifedata.com/resource/pubmed/commentcorrection/9501110-2734310, http://linkedlifedata.com/resource/pubmed/commentcorrection/9501110-2775186, http://linkedlifedata.com/resource/pubmed/commentcorrection/9501110-7396959, http://linkedlifedata.com/resource/pubmed/commentcorrection/9501110-7480322, http://linkedlifedata.com/resource/pubmed/commentcorrection/9501110-7640525, http://linkedlifedata.com/resource/pubmed/commentcorrection/9501110-7640526, http://linkedlifedata.com/resource/pubmed/commentcorrection/9501110-7757119, http://linkedlifedata.com/resource/pubmed/commentcorrection/9501110-7761437, http://linkedlifedata.com/resource/pubmed/commentcorrection/9501110-7866028, http://linkedlifedata.com/resource/pubmed/commentcorrection/9501110-7890741, http://linkedlifedata.com/resource/pubmed/commentcorrection/9501110-8400875, http://linkedlifedata.com/resource/pubmed/commentcorrection/9501110-8587994, http://linkedlifedata.com/resource/pubmed/commentcorrection/9501110-8934623, http://linkedlifedata.com/resource/pubmed/commentcorrection/9501110-8953244, http://linkedlifedata.com/resource/pubmed/commentcorrection/9501110-8989880
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/5-Methyltetrahydrofolate-Homocystein..., http://linkedlifedata.com/resource/pubmed/chemical/Acetolactate Synthase, http://linkedlifedata.com/resource/pubmed/chemical/Amino Acids, http://linkedlifedata.com/resource/pubmed/chemical/Aminobutyric Acids, http://linkedlifedata.com/resource/pubmed/chemical/Glutamate-Ammonia Ligase, http://linkedlifedata.com/resource/pubmed/chemical/Herbicides, http://linkedlifedata.com/resource/pubmed/chemical/Indoles, http://linkedlifedata.com/resource/pubmed/chemical/Nitrobenzoates, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger, http://linkedlifedata.com/resource/pubmed/chemical/Salicylic Acid, http://linkedlifedata.com/resource/pubmed/chemical/Salicylic Acids, http://linkedlifedata.com/resource/pubmed/chemical/Thiazoles, http://linkedlifedata.com/resource/pubmed/chemical/Tryptophan, http://linkedlifedata.com/resource/pubmed/chemical/acifluorfen, http://linkedlifedata.com/resource/pubmed/chemical/butyrine, http://linkedlifedata.com/resource/pubmed/chemical/camalexin
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
1040-4651
pubmed:author
pubmed:issnType
Print
pubmed:volume
10
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
359-70
pubmed:dateRevised
2010-9-10
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Induction of Arabidopsis tryptophan pathway enzymes and camalexin by amino acid starvation, oxidative stress, and an abiotic elicitor.
pubmed:affiliation
Boyce Thompson Institute for Plant Research and Section of Genetics and Development, Cornell University, Tower Road, Ithaca, New York 14853-1801, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.