Identification of the nuclear-encoded chloroplast ribosomal protein L12 of the monocotyledonous plant Secale cereale and sequencing of two different cDNAs with strong codon bias.
Two different cDNA clones (SCL12-1 and SCL12-2) encoding precursors of a chloroplast ribosomal protein with homology to L12 from Escherichia coli were isolated from rye leaf cDNA libraries and sequenced. The corresponding polypeptide of rye chloroplast ribosomes was identified. The sequences for the mature proteins of M(r) 13,447 and 13,609 share 85% amino acid identity. The mature polypeptide of clone SCL12-1 has an amino acid identity of 71%, 72% or 44%, respectively, relative to L12 proteins from spinach, tobacco, or E. coli. Codon usage of the rye L12 cDNAs shows a high preference (97% and 82%) for G or C in the third base position.
Schmidt
M
M
Botanisches Institut, J.W. Goethe-Universität, Frankfurt am Main, Germany.
Pichl
L
L
Lepper
M
M
Feierabend
J
J
D000595:Amino Acid Sequence; D001483:Base Sequence; D002736:Chloroplasts / Q000737:chemistry*; D003062:Codon; D008969:Molecular Sequence Data; D012269:Ribosomal Proteins; D012434:Secale / Q000235:genetics*
D003062:Codon; D012269:Ribosomal Proteins; C016700:ribosomal protein L7-L12