The Dapa Gene Encoding The Lysine Biosynthetic Enzyme Dihydrodipicolinate Synthase From Coix Lacryma-jobi: Cloning, Characterization, And Expression Analysis.

dc.creatorDante, R A
dc.creatorNeto, G C
dc.creatorLeite, A
dc.creatorYunes, J A
dc.creatorArruda, P
dc.date1999-Nov
dc.date2015-11-27T12:19:45Z
dc.date2015-11-27T12:19:45Z
dc.date.accessioned2018-03-29T00:53:52Z
dc.date.available2018-03-29T00:53:52Z
dc.identifierPlant Molecular Biology. v. 41, n. 4, p. 551-61, 1999-Nov.
dc.identifier0167-4412
dc.identifier
dc.identifierhttp://www.ncbi.nlm.nih.gov/pubmed/10608664
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/194457
dc.identifier10608664
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1294690
dc.descriptionDihydrodipicolinate 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.
dc.description41
dc.description551-61
dc.languageeng
dc.relationPlant Molecular Biology
dc.relationPlant Mol. Biol.
dc.rightsfechado
dc.rights
dc.sourcePubMed
dc.subjectAmino Acid Sequence
dc.subjectBase Sequence
dc.subjectCloning, Molecular
dc.subjectDna, Plant
dc.subjectDna-binding Proteins
dc.subjectGene Dosage
dc.subjectGene Expression Regulation, Developmental
dc.subjectGene Expression Regulation, Enzymologic
dc.subjectGene Expression Regulation, Plant
dc.subjectGenes
dc.subjectHydro-lyases
dc.subjectLight
dc.subjectLysine
dc.subjectMolecular Sequence Data
dc.subjectPlant Proteins
dc.subjectPoaceae
dc.subjectRna, Messenger
dc.subjectSequence Alignment
dc.subjectSequence Analysis, Dna
dc.subjectSequence Homology, Amino Acid
dc.subjectTissue Distribution
dc.subjectTranscription Factors
dc.subjectZea Mays
dc.titleThe Dapa Gene Encoding The Lysine Biosynthetic Enzyme Dihydrodipicolinate Synthase From Coix Lacryma-jobi: Cloning, Characterization, And Expression Analysis.
dc.typeArtículos de revistas


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