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. 1977 Aug;86(4):745–764. doi: 10.1093/genetics/86.4.745

Frameshifts and Frameshift Suppressors in SACCHAROMYCES CEREVISIAE

Michael R Culbertson 1, Lawrence Charnas 1, M Tina Johnson 1, Gerald R Fink 1
PMCID: PMC1213708  PMID: 72702

Abstract

Using ICR-170 as a mutagen, we have induced a set of mutations in yeast which exhibit behavior similar to that shown for bacterial frameshift mutations. Our genetic study shows that these mutations are polar; the polarity can be relieved by internal suppressors; they revert with acridine half-mustards and are not suppressed by known nonsense suppressors. However, they are suppressed by other dominant external suppressors, which fall into two mutually exclusive groups. Five genetically distinct suppressors were obtained for one of these groups, using co-reversion of two frameshift markers. Three of these are lethal in combination with each other and show a reduction in the GLY3 tRNA peak on a Sepharose 4B column. A fourth suppressor shows an altered chromatographic profile for GLY1 tRNA. We suggest that this group of suppressors represent mutations in the structural genes for the isoaccepting glycyl-tRNA's. Two other suppressors (one linked to the centromere of chromosome III) were found to suppress a second group of frameshifts. Genetic and biochemical studies show that the nonMendelian factor [PSI+] increases the efficiency of some frameshift suppressors.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. CARLSON E. A., OSTER I. I. Comparative mutagenesis of the dumpy locus in Drosophila melanogaster. II. Mutational mosaicism induced without apparent breakage by a monofunctional alkylating agent. Genetics. 1962 May;47:561–576. doi: 10.1093/genetics/47.5.561. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. CRICK F. H., BARNETT L., BRENNER S., WATTS-TOBIN R. J. General nature of the genetic code for proteins. Nature. 1961 Dec 30;192:1227–1232. doi: 10.1038/1921227a0. [DOI] [PubMed] [Google Scholar]
  3. Cieslà Z., Salvatore F., Broach J. R., Artz S. W., Ames B. N. Histidine regulation in Salmonella typhimurium. XVI. A sensitive radiochemical assay for histidinol dehydrogenase. Anal Biochem. 1975 Jan;63(1):44–55. doi: 10.1016/0003-2697(75)90187-6. [DOI] [PubMed] [Google Scholar]
  4. Cox B. S. A recessive lethal super-suppressor mutation in yeast and other psi phenomena. Heredity (Edinb) 1971 Apr;26(2):211–232. doi: 10.1038/hdy.1971.28. [DOI] [PubMed] [Google Scholar]
  5. Liebman S. W., Stewart J. W., Sherman F. Serine substitutions caused by an ochre suppressor in yeast. J Mol Biol. 1975 Jun 5;94(4):595–610. doi: 10.1016/0022-2836(75)90324-1. [DOI] [PubMed] [Google Scholar]
  6. Malling H. V. The mutagenicity of the acridine mustard (ICR-170) and the structurally related compounds in Neurospora. Mutat Res. 1967 May-Jun;4(3):265–274. doi: 10.1016/0027-5107(67)90021-8. [DOI] [PubMed] [Google Scholar]
  7. Pearson R. L., Weiss J. F., Kelmers A. D. Improved separation of transfer RNA's on polychlorotrifuoroethylene-supported reversed-phase chromatography columns. Biochim Biophys Acta. 1971 Feb 11;228(3):770–774. doi: 10.1016/0005-2787(71)90748-9. [DOI] [PubMed] [Google Scholar]
  8. Riddle D. L., Carbon J. Frameshift suppression: a nucleotide addition in the anticodon of a glycine transfer RNA. Nat New Biol. 1973 Apr 25;242(121):230–234. doi: 10.1038/newbio242230a0. [DOI] [PubMed] [Google Scholar]
  9. Riddle D. L., Roth J. R. Suppressors of frameshift mutations in Salmonella typhimurium. J Mol Biol. 1970 Nov 28;54(1):131–144. doi: 10.1016/0022-2836(70)90451-1. [DOI] [PubMed] [Google Scholar]
  10. Yourno J. Similarity of cross-suppressible frameshifts in Salmonella typhimurium. J Mol Biol. 1971 Nov 28;62(1):223–231. doi: 10.1016/0022-2836(71)90141-0. [DOI] [PubMed] [Google Scholar]

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