Strong homology between the small subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase of two species of Acetabularia and the occurrence of unusual codon usage.
Amino acid sequences of the small subunit of ribulose-1,5-bisphosphate carboxylase (SSU) of Acetabularia cliftonii and A. mediterranea were derived from five cDNA sequences of each of the two species of algae and by direct amino acid sequence determination of the isolated protein. An homology of more than 96% between the proteins indicates the close relationship between the two algae. All ten cDNAs in the reading frame display the termination codons TAA and/or TAG at various positions, which seem to code for the amino acid glutamine when compared with the amino acid sequence from the mature protein. This is reminiscent of proteins from ciliates where TAA and TAG also code for glutamine.
Schneider
S U
SU
Max-Planck-Institut für Zellbiologie, Abteilung Schweiger, Ladenburg, Federal Republic of Germany.
Leible
M B
MB
Yang
X P
XP
D000076:Acetabularia / Q000235:genetics*; D000595:Amino Acid Sequence; D001483:Base Sequence; D000460:Chlorophyta / Q000235:genetics*; D003062:Codon; D004247:DNA / Q000032:analysis*; D005973:Glutamine / Q000235:genetics*; D008969:Molecular Sequence Data; D009693:Nucleic Acid Hybridization; D012150:Polymorphism, Restriction Fragment Length; D012333:RNA, Messenger; D012273:Ribulose-Bisphosphate Carboxylase / Q000235:genetics*; D012689:Sequence Homology, Nucleic Acid
D003062:Codon; D012333:RNA, Messenger; D005973:Glutamine; D004247:DNA; D012273:Ribulose-Bisphosphate Carboxylase