Characterization of cDNA clones encoding the human homologue of Saccharomyces cerevisiae ribosomal protein L30

Research output: Contribution to journalArticle

6 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)283-285
Number of pages3
JournalGene
Volume123
Issue number2
DOIs
StatePublished - Jan 30 1993

Fingerprint

Saccharomyces cerevisiae Proteins
Fungal Proteins
Complementary DNA
Clone Cells
Immunoglobulin Heavy Chains
Messenger RNA
Ribosomal Proteins
Xenopus laevis
Codon
Open Reading Frames
Nucleotides
Cell Culture Techniques
Yeasts
ribosomal protein L30
pyrimidine

Keywords

  • Xenopus laevis
  • Yeast
  • cloning
  • ribosomes

ASJC Scopus subject areas

  • Genetics

Cite this

Characterization of cDNA clones encoding the human homologue of Saccharomyces cerevisiae ribosomal protein L30. / Johnson, Keith R.

In: Gene, Vol. 123, No. 2, 30.01.1993, p. 283-285.

Research output: Contribution to journalArticle

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