Functional substitution of mouse ribosomal protein L27' for yeast ribosomal protein L29 in yeast ribosomes.
AUTOR(ES)
Fleming, G
RESUMO
A cDNA clone of mouse ribosomal protein L27' was shown previously to be 62% identical in amino acid residues to yeast ribosomal protein L29. The L27' cDNA was expressed in yeast to determine the ability of the mouse protein to substitute for yeast L29 in assembling a functional ribosome. In a yeast strain resistant to cycloheximide by virtue of a recessive mutation in the L29 protein, the murine cDNA did not produce a sensitive phenotype, indicating failure of the mouse L27' protein to assemble into yeast ribosomes. However, when the mouse L27' gene was expressed in cells devoid of L29 and otherwise inviable, the murine protein supported normal growth, demonstrating that mouse ribosomal protein L27' indeed was interchangeable with yeast L29. We conclude that mouse ribosomal protein L27' is assembled into ribosomes in yeast, but yeast L29 is assembled preferentially when both L29 and L27' are present in the same cell.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=286435Documentos Relacionados
- Subpopulations of chloroplast ribosomes change during photoregulated development of Zea mays leaves: Ribosomal proteins L2, L21, and L29
- Isolation and characterisation of a murine cDNA clone highly homologous to the yeast L29 ribosomal protein gene.
- Interaction of Escherichia coli ribosomal protein S1 with ribosomes.
- Molecular cloning and analysis of yeast gene for cycloheximide resistance and ribosomal protein L29.
- Two genes for ribosomal protein 51 of Saccharomyces cerevisiae complement and contribute to the ribosomes.
