The primary structure of rat ribosomal protein L5. A comparison of the sequence of amino acids in the proteins that interact with 5 S rRNA.

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DOI: 10.1016/S0021-9258(18)45288-X

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摘要: The covalent structure of rat ribosomal protein L5, which associates with 5 S rRNA in the organelle, was deduced from sequence nucleotides a recombinant cDNA (pL5-6-4) and confirmed sequences amino acids portions protein. Ribosomal encoded by pL5-6-4, contains 296 has molecular weight 34,298. However, second cDNA, pL5-8-5, encodes an additional methionyl residue at position 236 may be product active L5 gene. Rat is homologous to yeast YL3 Halobacterium cutirubrum HL13, proteins that also bind rRNA. No significant structural similarity, however, found between other rRNA-binding proteins; not H. HL19, nor Escherichia coli proteins, L18, or L25, Xenopus laevis transcription factor IIIA. identity E. seems related and, hence, evolutionary link prokaryotic eukaryotic proteins. A group known associated are L5. They include: L39, Euglina gracilis chloroplast S7, Saccharomyces cerevisiae L31 L46, Homo sapiens L32 perhaps, several others as well. There especially close interrelationship human L32, mouse L32. These results, others, suggest form extended family contain its traces this affinity.

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