Proteins of cytoplasmic ribosomes of the Podospora anserina were analyzed by two dimensional gel electrophoresis. The numbers of proteins were estimated to be 28 in the small subunit and 41 in the large subunit. The L21 protein of the large subunit was found to migrate differently in a cycloheximide
Altered ribosomal protein L29 in a cycloheximide-resistant strain ofSaccharomyces cerevisiae
✍ Scribed by Walter Stöcklein; Wolfgang Piepersberg
- Publisher
- Springer-Verlag
- Year
- 1980
- Tongue
- English
- Weight
- 793 KB
- Volume
- 1
- Category
- Article
- ISSN
- 0172-8083
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✦ Synopsis
A spontaneous high-level cycloheximide-resistant mutant of the yeast Saccharomyces cerevisiae (strain cy32) is found to have an altered protein of the large subunit (60S) of cytoplasmic ribosomes, namely protein L29. The resistance character segregates together with this biochemical defect and is semidominant in heterozygous diploids. Judged from in vitro susceptibility to inhibition by cycloheximide there are at least 50% resistant ribosomes present in such diploid strains. From these results it is concluded that cycloheximide resistance of mutant cy32 is caused by mutation of a single gene and that it is the structural gene for L29 which is affected.Preliminary genetic mapping data are also reported. They indicate a location of cyhx-32 marker on chromosome 7 near met13.
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