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Molecular characterization of the spinach G‐box binding protein family
Author(s) -
Bolle Cordelia,
Lübberstedt Thomas,
Herranen Mirkka,
Herrmann Reinhold G.,
Oelmüller Ralf
Publication year - 1998
Publication title -
physiologia plantarum
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.351
H-Index - 146
eISSN - 1399-3054
pISSN - 0031-9317
DOI - 10.1034/j.1399-3054.1998.1030315.x
Subject(s) - biology , gene , pseudogene , genetics , promoter , bzip domain , leucine zipper , spinach , microbiology and biotechnology , gene family , gene cluster , gene expression , peptide sequence , biochemistry , genome
The promoters of the spinach ferredoxin‐NADP + ‐oxidoreductase gene and one member of the gene family for the small subunit of ribulose‐1,5‐bisphosphate carboxylase contain ACGT sequences relevant for gene expression. Site‐directed mutagenesis revealed that these sequences operate quantitatively and are not involved in the light response. We have isolated a cDNA for a basic leucine zipper protein (bZIP) from spinach. After transcription and translation in cell‐free systems, the protein binds in vitro to double‐stranded oligonucleotides designed according to both sequences, although with different efficiencies. The genomic DNA segment for this bZIP contains 10 introns. The bZIP gene promoter harbors also an ACGT sequence; however, promoter/ uidA gene fusions revealed that these nucleotides are not essential for expression. At least three other genes with high similarities are present in the spinach genome; however, they appear to be either pseudogenes, because they contain in‐frame stop codons in highly conserved epitopes, or must be posttranscriptionally modified in order to code for functional proteins. The high sequence similarities suggest that all four sequences derive from gene duplications.