Nm. Willingham et al., MOLECULAR-CLONING OF THE ARABIDOPSIS-THALIANA SEDOHEPTULOSE-1,7-BIPHOSPHATASE GENE AND EXPRESSION STUDIES IN WHEAT AND ARABIDOPSIS-THALIANA, Plant molecular biology, 26(4), 1994, pp. 1191-1200
We report here the isolation and nucleotide sequence of genomic clones
encoding the chloroplast enzyme sedoheptulose-1,7-bisphosphatase (SBP
ase) from Arabidopsis thaliana. The coding region of this gene contain
s eight exons (72-76 bp) and seven introns (75-91 bp) and encodes a po
lypeptide of 393 amino acids. Unusually, the 5' non-coding region cont
ains two additional AUG codons upstream of the translation initiation
codon. A comparison of the deduced Arabidopsis and wheat SBPase polype
ptide sequences reveals 78.6%, identity. Expression studies showed tha
t the level of SBPase mRNA in Arabidopsis and wheat is regulated in a
light-dependent manner and is also influenced by the developmental sta
ge of the leaf. Although the Arabidopsis SBPase gene is present in a s
ingle copy, two hybridizing transcripts were detected in some tissues,
suggesting the presence of alternate transcription start sites in the
upstream region.