ArticlePlant molecular biology1999
The DapA gene encoding the lysine biosynthetic enzyme dihydrodipicolinate synthase from Coix lacryma-jobi: cloning, characterization, and expression analysis.
Article in Plant molecular biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 15 citations in OpenAlex.
- The Hidden Potential of High-Throughput RNA-Seq Re-Analysis, a Case Study for DHDPS, Key Enzyme of the Aspartate-Derived Lysine Biosynthesis Pathway and Its Role in Abiotic and Biotic Stress Responses in Soybean.Plants (Basel, Switzerland) · 2022Article
- Adlay, an ancient functional plant with nutritional quality, improves human health.Frontiers in nutrition · 2022Review
- Novel insights into host-pathogen interactions of large yellow croakers (Zoological research · 2020Article
- Medicago truncatula dihydrodipicolinate synthase (DHDPS) enzymes display novel regulatory properties.Plant molecular biology · 2013Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Dihydrodipicolinate synthase (DHPS) is the main enzyme of a specific branch of the aspartate pathway leading to lysine biosynthesis in higher plants. We have cloned and characterized the DHPS-encoding Dap)A gene from the maize-related grass Coix lacryiana-jobi. The DapA open reading frame is interrupted by two introns and encodes the 326 amino acid-long Coix DHPS protein, which is 95% identical to the maize DHPS protein. Coix DNA gel blot analysis with maize DHPS cDNA as a probe showed a single strongly hybridizing band along with faint bands. RNA gel blot analysis showed that DHPS transcripts are present in coleoptiles, embryos, endosperms, and roots but are almost undetectable in blades of young leaves of both Coix and maize. The 5'-flanking region of the DapA gene contains a TGACTC GCN4-like element located 372 bp upstream the putative translation start codon. Steady-state levels of DHPS mRNA were slightly reduced in the endosperms and embryos of the maize lysine-rich opaque2 mutants when compared with those in normal kernels. Selective binding assay with the maize Opaque2 protein (O2) showed that the GCN4-like element is not an O2 binding site, suggesting that the DHPS gene is not under the control of O2.
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