Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/194457
Type: Artigo de periódico
Title: The Dapa Gene Encoding The Lysine Biosynthetic Enzyme Dihydrodipicolinate Synthase From Coix Lacryma-jobi: Cloning, Characterization, And Expression Analysis.
Author: Dante, R A
Neto, G C
Leite, A
Yunes, J A
Arruda, P
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.
Subject: Amino Acid Sequence
Base Sequence
Cloning, Molecular
Dna, Plant
Dna-binding Proteins
Gene Dosage
Gene Expression Regulation, Developmental
Gene Expression Regulation, Enzymologic
Gene Expression Regulation, Plant
Genes
Hydro-lyases
Light
Lysine
Molecular Sequence Data
Plant Proteins
Poaceae
Rna, Messenger
Sequence Alignment
Sequence Analysis, Dna
Sequence Homology, Amino Acid
Tissue Distribution
Transcription Factors
Zea Mays
Citation: Plant Molecular Biology. v. 41, n. 4, p. 551-61, 1999-Nov.
Rights: fechado
Identifier DOI: 
Address: http://www.ncbi.nlm.nih.gov/pubmed/10608664
Date Issue: 1999
Appears in Collections:Unicamp - Artigos e Outros Documentos

Files in This Item:
File SizeFormat 
pmed_10608664.pdf256.1 kBAdobe PDFView/Open


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.