The primary structure of rat ribosomal protein L12.
The covalent structure of the rat 60S subunit protein L12 which is a component of the ribosomal elongation factor binding domain was deduced from the sequence of nucleotides in a recombinant cDNA and confirmed from the NH2-terminal amino acid sequence of the protein. L12 has 165 amino acids and a molecular weight of 17,834. Hybridization of the cDNA to digests of nuclear DNA suggests that there are 11-13 copies of the L12 gene. The mRNA for the protein is about 800 nucleotides in length. Rat L12 is homologous to Saccharomyces cerevisiae L15. The cDNA contains the highly repetitive DNA sequence, R.dre.1, in the 3' noncoding region.
Suzuki
K
K
Department of Biochemistry and Molecular Biology, University of Chicago, Illinois 60637.
Olvera
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Wool
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D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D004274:DNA, Recombinant / Q000032:analysis; D015723:Gene Library; D008099:Liver / Q000378:metabolism; D008969:Molecular Sequence Data; D009693:Nucleic Acid Hybridization; D015345:Oligonucleotide Probes; D011061:Poly A / Q000235:genetics / Q000302:isolation & purification; D012333:RNA, Messenger / Q000235:genetics / Q000302:isolation & purification; D051381:Rats; D012269:Ribosomal Proteins / Q000737:chemistry / Q000235:genetics*
D004274:DNA, Recombinant; D015345:Oligonucleotide Probes; D012333:RNA, Messenger; D012269:Ribosomal Proteins; D011061:Poly A; C016700:ribosomal protein L7-L12