The Gene and the Primary Structure of Acidic Ribosomal Protein AO from Yeast Saccharomyces cerevisiae Which Shows Partial Homology to Bacterial Ribosomal Protein L101
- 1 August 1989
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 106 (2) , 223-227
- https://doi.org/10.1093/oxfordjournals.jbchem.a122836
Abstract
Eukaryotic ribosomes contain an acidic ribosomal protein of about 38 kDa which shows immunological cross-reactivity with the 13 kDa-type acidic ribosomal proteins that are related to L7/L12 of bacterial ribosomes. By using a cDNA clone for 38 kDa-type acidic ribosomal protein AO from the yeast Saccharomyces cerevisiae, we have cloned a genomic DNA encoding AO and determined the sequence of 1, 614 nucleotides including about 500 nucleotides in the 5 -flanking region. The gene lacks introns and possesses two boxes homologous to upstream activation sequences (UASrpg) in the 5 -flanking region. The amino acid sequence of AO deduced from the nucleotide sequence shows that AO shares a highly similar carboxyl-tenninal region of about 40 amino acids in length with 13 kDa-type acidic ribosomal proteins, including an identical carboxyl-terminai, DDDMGFGLFD. In the amino-terminal region AO contains an arginine-rich segment which shows a low but distinct similarity to that of bacterial ribosomal protein L10 through which L10 is thought to bind to 23S rRNA. On the other hand, the carboxyl-terminai half of AO is enriched with hydrophobic amino acid residues including four pairs of phenylalanine residues which are all conserved in a human homologue.Keywords
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