ArticlePlant molecular biology2010
Lysine racemase: a novel non-antibiotic selectable marker for plant transformation.
Article in Plant molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 39 citations in OpenAlex.
- Methylglyoxal-glyoxalase system as a possible selection module for raising marker-safe plants in rice.Physiology and molecular biology of plants : an international journal of functional plant biology · 2021Article
- Plant-associated and soil microbiota composition as a novel criterion for the environmental risk assessment of genetically modified plants.GM crops & food · 2020Article
- New Insights Into the Mechanisms and Biological Roles of D-Amino Acids in Complex Eco-Systems.Frontiers in microbiology · 2018Review
- Widespread Inter- and Intra-Domain Horizontal Gene Transfer of d-Amino Acid Metabolism Enzymes in Eukaryotes.Frontiers in microbiology · 2016Article
- Synthetic biology approaches to improve biocatalyst identification in metagenomic library screening.Microbial biotechnology · 2015Review
- Analyses of Arabidopsis ecotypes reveal metabolic diversity to convert D-amino acids.SpringerPlus · 2013Article
- Recent advances in development of marker-free transgenic plants: regulation and biosafety concern.Journal of biosciences · 2012Review
- Crystal structures of lysine-preferred racemases, the non-antibiotic selectable markers for transgenic plants.PloS one · 2012Article
- Genetically modified foods and social concerns.Avicenna journal of medical biotechnology · 2011Article
- Metagenomic analyses: past and future trends.Applied and environmental microbiology · 2011Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A non-antibiotic based selection system using L-lysine as selection agent and the lysine racemase (lyr) as selectable marker gene for plant transformation was established in this study. L-lysine was toxic to plants, and converted by Lyr into D-lysine which would subsequently be used by the transgenic plants as nitrogen source. Transgenic tobacco and Arabidopsis plants were successfully recovered on L-lysine medium at efficiencies of 23 and 2.4%, respectively. Phenotypic characterization of transgenic plants clearly revealed the expression of normal growth and developmental characteristics as that of wild-type plants, suggesting no pleiotropic effects associated with the lyr gene. The specific activity of Lyr in transgenic tobacco plants selected on L: -lysine ranged from 0.77 to 1.06 mU/mg protein, whereas no activity was virtually detectable in the wild-type plants. In addition, the composition of the free amino acids, except aspartic acid, was not affected by the expression of the lyr gene in the transgenic tobacco plants suggesting very limited interference with endogenous amino acid metabolism. Interestingly, our findings also suggested that the plant aspartate kinases may possess an ability to distinguish the enantiomers of lysine for feedback regulation. To our knowledge, this is the first report to demonstrate that the lysine racemase selectable marker system is novel, less controversial and inexpensive than the traditional selection systems.
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