The DapA gene encoding the lysine biosynthetic enzyme dihydrodipicolinate synthase from Coix lacryma-jobi: cloning, characterization, and expression analysis

dc.creatorDante, RA
dc.creatorNeto, GC
dc.creatorLeite, A
dc.creatorYunes, JA
dc.creatorArruda, P
dc.date1999
dc.dateNOV
dc.date2014-12-02T16:30:13Z
dc.date2015-11-26T17:39:18Z
dc.date2014-12-02T16:30:13Z
dc.date2015-11-26T17:39:18Z
dc.date.accessioned2018-03-29T00:20:54Z
dc.date.available2018-03-29T00:20:54Z
dc.identifierPlant Molecular Biology. Kluwer Academic Publ, v. 41, n. 4, n. 551, n. 561, 1999.
dc.identifier0167-4412
dc.identifierWOS:000083831700011
dc.identifier10.1023/A:1006367116073
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/74900
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/74900
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/74900
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1286422
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 DapA gene from the maize-related grass Coix lacryma-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.description4
dc.description551
dc.description561
dc.languageen
dc.publisherKluwer Academic Publ
dc.publisherDordrecht
dc.publisherHolanda
dc.relationPlant Molecular Biology
dc.relationPlant Mol.Biol.
dc.rightsfechado
dc.sourceWeb of Science
dc.subjectCoix lacryma jobi
dc.subjectdihydrodipicolinate synthase
dc.subjectGCN4
dc.subjectlysine
dc.subjectmaize
dc.subjectopaque2
dc.subjectHomoserine Dehydrogenase Gene
dc.subjectTranscriptional Activator Opaque-2
dc.subjectInsensitive Aspartate Kinase
dc.subjectAmino-acid Biosynthesis
dc.subjectNicotiana-sylvestris
dc.subjectHigher-plants
dc.subjectKetoglutarate Reductase
dc.subjectArabidopsis-thaliana
dc.subjectThreonine Synthesis
dc.subjectMaize Endosperms
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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