Characterization of a cycloheximide-resistant Tetrahymena thermophila mutant which also displays altered growth properties.
Open Access
- 1 April 1983
- journal article
- research article
- Published by Taylor & Francis in Molecular and Cellular Biology
- Vol. 3 (4) , 503-510
- https://doi.org/10.1128/mcb.3.4.503
Abstract
A cycloheximide-resistant strain of Tetrahymena thermophila, expressing a mutant chx-B gene (Ares and Bruns, Genetics 90:463-474, 1978), displayed very different temperature-dependent growth characteristics than either wild-type cells or another cycloheximide-resistant strain expressing a different mutant gene. Whereas wild-type cells showed an immediate decline in ribosome translocation rates when shifted from 30 to 38 or 40 degrees C, this mutant strain (X-8) showed no such decline. These results directly correlated with the growth rate differences we found for these cells at these temperatures. By genetic analysis, we showed that the phenotype of cycloheximide resistance cosegregated with the ability to grow rapidly at 40 degrees C. Analyses, both direct and indirect, suggested that a number of functional and structural characteristics of the ribosomes from strain X-8 cells are most likely conformationally different from those of wild-type ribosomes.This publication has 20 references indexed in Scilit:
- Heat shock induces rapid dephosphorylation of a ribosomal protein in Drosophila.Proceedings of the National Academy of Sciences, 1982
- Regulation of ribosome phosphorylation and antibiotic sensitivity in tetrahymena thermophila: A correlationCell, 1981
- Cloning of yeast gene for trichodermin resistance and ribosomal protein L3.Proceedings of the National Academy of Sciences, 1981
- Binding of cycloheximide to ribosomes from wild-type and mutant strains of Saccharomyces cerevisiaeAntimicrobial Agents and Chemotherapy, 1980
- Translational control of protein synthesis in response to heat shock in D. melanogaster cellsCell, 1980
- Heat shock, deciliation and release from anoxia induce the synthesis of the same set of polypeptides in starved T. pyriformisCell, 1980
- The Structure and Function of Eukaryotic RibosomesAnnual Review of Biochemistry, 1979
- Characterization of ribosomal precursor particles from HeLa cell nucleoliJournal of Molecular Biology, 1972
- Regulation of protein synthesis in mammalian cellsJournal of Molecular Biology, 1970
- THE GENETICS OF THE H SEROTYPE SYSTEM IN VARIETY 1 OF TETRAHYMENA PYRIFORMISGenetics, 1960