title: Characterization of cDNA clones encoding the human homologue of Saccharomyces cerevisiae ribosomal protein L30.
abstract: We have isolated cDNA clones encoding the human homologue (hL30) of yeast ribosomal protein (r-protein) L30. The hL30 nucleotide (nt) sequence shows high homology to the yeast sequences and also to a partial Xenopus laevis sequence previously identified as an immunoglobulin heavy chain. The 5' end of hL30 is pyrimidine-rich, as is the case for most other mammalian r-protein mRNAs. The open reading frame consists of 157 codons with a C-terminal region that is different from corresponding regions of the yeast proteins. In several human tissue culture cells, the mRNA encoding hL30 is approx. 700 nt in length.
authors.affiliation: Department of Biology, University of Toledo, OH 43606.
authors.forename: K R
authors.initials: KR
authors.lastname: Johnson
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D006801:Humans; D007143:Immunoglobulin Heavy Chains / Q000235:genetics; D008969:Molecular Sequence Data; D012269:Ribosomal Proteins / Q000235:genetics*; D012441:Saccharomyces cerevisiae; D017386:Sequence Homology, Amino Acid; D014982:Xenopus laevis
chemical_list: D007143:Immunoglobulin Heavy Chains; D012269:Ribosomal Proteins; C035201:ribosomal protein L30