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Threonine accumulation in a mutant of Arabidopsis thaliana (L.) Heynh. with an altered aspartate kinase

Betty Heremans UGent and Michel Jacobs (1995) JOURNAL OF PLANT PHYSIOLOGY. 146(3). p.249-257
abstract
After mutagenesis, M(2) seedlings of Arabidopsis thaliana were grown on a selective medium containing toxic concentrations of lysine and threonine. One of the LT-resistant mutants (RLT 40) was studied at the biochemical and genetical levels. A six-fold increase in free threonine content was found in 8-day-old mutant plantlets compared with the wild type. The total amino acid content of the mutant was also remarkably increased, essentially due to increased levels of aspartate, threonine, methionine, isoleucine and lysine. As one of the possible reasons for the LT-resistance resides in a change of the regulatory properties of the first enzyme of the aspartate pathway, aspartate kinase (EC 2.7.2.4), the feedback-inhibition pattern of aspartate kinase was examined in the mutant and the wild type. In Arabidopsis after ion-exchange chromatography of whole plant extracts, three peaks of activity were detected corresponding respectively to a threonine-sensitive isoform, to a lysine-sensitive form and a form insensitive to both inhibitors. The threonine accumulation in RLT 40 could be related to a partial insensitivity of the lysine-sensitive form of aspartate kinase. Genetical analysis showed that the resistance gene behaved as a dominant, monogenic nuclear trait. Linkage analysis, performed with a multiple marker line, indicated that the mutation is located on chromosome 2, 36.0 cM from the er locus and 19.8 cM from the py locus on chromosome 2. This partially lysine-insensitive mutant of aspartate kinase offers ways to a map-based approach for cloning the gene coding for the corresponding isoform in plants.
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (original)
publication status
published
subject
keyword
ASPARTOKINASE, RESISTANT, ISOENZYMES, LYSINE PLUS THREONINE, POLYMORPHISM LINKAGE MAP, THREONINE OVERPRODUCTION, LT-RESISTANCE, ARABIDOPSIS THALIANA (L) HEYNH, ASPARTATE KINASE, CLONING, PROTEIN, GENOME, MAIZE, GENE
journal title
JOURNAL OF PLANT PHYSIOLOGY
J. Plant Physiol.
volume
146
issue
3
pages
249 - 257
Web of Science type
Article
ISSN
0176-1617
language
English
UGent publication?
no
classification
A1
id
770424
handle
http://hdl.handle.net/1854/LU-770424
date created
2009-10-28 14:08:33
date last changed
2009-11-30 14:09:29
@article{770424,
  abstract     = {After mutagenesis, M(2) seedlings of Arabidopsis thaliana were grown on a selective medium containing toxic concentrations of lysine and threonine. One of the LT-resistant mutants (RLT 40) was studied at the biochemical and genetical levels. A six-fold increase in free threonine content was found in 8-day-old mutant plantlets compared with the wild type. The total amino acid content of the mutant was also remarkably increased, essentially due to increased levels of aspartate, threonine, methionine, isoleucine and lysine. As one of the possible reasons for the LT-resistance resides in a change of the regulatory properties of the first enzyme of the aspartate pathway, aspartate kinase (EC 2.7.2.4), the feedback-inhibition pattern of aspartate kinase was examined in the mutant and the wild type. In Arabidopsis after ion-exchange chromatography of whole plant extracts, three peaks of activity were detected corresponding respectively to a threonine-sensitive isoform, to a lysine-sensitive form and a form insensitive to both inhibitors. The threonine accumulation in RLT 40 could be related to a partial insensitivity of the lysine-sensitive form of aspartate kinase.
Genetical analysis showed that the resistance gene behaved as a dominant, monogenic nuclear trait. Linkage analysis, performed with a multiple marker line, indicated that the mutation is located on chromosome 2, 36.0 cM from the er locus and 19.8 cM from the py locus on chromosome 2. This partially lysine-insensitive mutant of aspartate kinase offers ways to a map-based approach for cloning the gene coding for the corresponding isoform in plants.},
  author       = {Heremans, Betty and Jacobs, Michel},
  issn         = {0176-1617},
  journal      = {JOURNAL OF PLANT PHYSIOLOGY},
  keyword      = {ASPARTOKINASE,RESISTANT,ISOENZYMES,LYSINE PLUS THREONINE,POLYMORPHISM LINKAGE MAP,THREONINE OVERPRODUCTION,LT-RESISTANCE,ARABIDOPSIS THALIANA (L) HEYNH,ASPARTATE KINASE,CLONING,PROTEIN,GENOME,MAIZE,GENE},
  language     = {eng},
  number       = {3},
  pages        = {249--257},
  title        = {Threonine accumulation in a mutant of Arabidopsis thaliana (L.) Heynh. with an altered aspartate kinase},
  volume       = {146},
  year         = {1995},
}

Chicago
Heremans, Betty, and Michel Jacobs. 1995. “Threonine Accumulation in a Mutant of Arabidopsis Thaliana (L.) Heynh. with an Altered Aspartate Kinase.” Journal of Plant Physiology 146 (3): 249–257.
APA
Heremans, B., & Jacobs, M. (1995). Threonine accumulation in a mutant of Arabidopsis thaliana (L.) Heynh. with an altered aspartate kinase. JOURNAL OF PLANT PHYSIOLOGY, 146(3), 249–257.
Vancouver
1.
Heremans B, Jacobs M. Threonine accumulation in a mutant of Arabidopsis thaliana (L.) Heynh. with an altered aspartate kinase. JOURNAL OF PLANT PHYSIOLOGY. 1995;146(3):249–57.
MLA
Heremans, Betty, and Michel Jacobs. “Threonine Accumulation in a Mutant of Arabidopsis Thaliana (L.) Heynh. with an Altered Aspartate Kinase.” JOURNAL OF PLANT PHYSIOLOGY 146.3 (1995): 249–257. Print.