Reference "Structure and some characterization of the gene for phenylalanine ammonia-lyase from rice plants"

Reference ID

2791

Title

Structure and some characterization of the gene for phenylalanine ammonia-lyase from rice plants

Source

European journal of biochemistry / FEBS, 1989, vol. 185, pp. 19-25

Authors (5)

Minami-E	Ozeki-Y
Matsuoka-M	Koizuka-N
Tanaka-Y

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.