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  • Title: Structure and some characterization of the gene for phenylalanine ammonia-lyase from rice plants.
    Author: Minami E, Ozeki Y, Matsuoka M, Koizuka N, Tanaka Y.
    Journal: Eur J Biochem; 1989 Oct 20; 185(1):19-25. PubMed ID: 2806257.
    Abstract:
    A nearly full-length cDNA and a genomic clone were isolated that encoded the phenylalanine ammonia-lyase (PAL) of rice plants, and the complete nucleotide sequences were determined. The gene encodes a polypeptide of 701 amino acid residues. The deduced amino acid sequence is highly similar to that of PAL from Phaseolus vulgaris deduced from an incomplete cDNA fragment. The cloned gene spans 4412 bp and consists of two exons and one intron. The site of initiation of transcription was located -86 nucleotides (position 1) upstream from the translational initiation codon by the primer-extension method. Sequences analogous to TATA-box and GC-box were found in the 5'-upstream region from the transcriptional initiation site. Southern blot analysis showed that the PAL gene of rice plants exists as a small multi-gene family. Within this family, the genomic clone isolated in this study was shown to be responsive by light. This also indicated that this genomic sequence functions as a gene for phenylalanine ammonia-lyase in rice plants in vivo.
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