Jm. Bae et al., CLONING AND CHARACTERIZATION OF PLASTID RIBOSOMAL-PROTEIN S16 GENE FROM POTATO (SOLANUM-TUBEROSUM L. CV DESIREE), Molecules and Cells, 8(4), 1998, pp. 466-470
The plastid ribosomal protein s16 (rps16) gene was cloned from potato
(Solanum tuberosum L. ssp. tuberosum cv Desiree) by PCR amplification
to obtain a new homologous recombination site of plastid transformatio
n. The potato rps16 genomic clone was 1627 bp in size and the coding r
egion was interrupted by an 859 bp intron. Exon I was 40 bp, encoding
13 amino acids and exon II was 227 bp, encoding a 76 amino acid polype
ptide, The nucleotide sequence of the rps16 gene from the ''Desiree''
potato shared perfect identity with the sequence from the ''Superior''
potato in the coding region, Three nucleotide substitutions, two nucl
eotide insertions, and one nucleotide deletion mere found between the
intron sequence of both ''Desiree'' and ''Superior'' cultivars. The am
ino acid sequence of the potato rps16 gene showed a high level of iden
tity with rice, maize, tobacco, and mustard (84-94%) and a relatively
low level compared with Bacillus stearothermophilus and E. coli (27-28
%). Expression of the rps16 gene was strong in chloroplasts and transc
ripts were delectable in amylopasts, suggesting that the rps16 gene is
active in nonphotosynthetic plastids as well as in photosynthetic pla
stids. These results indicate that the potato rps16 gene can be used a
s a new homologous recombination site of plastid transformation for po
tato cultivars.