Literature DB >> 11436550

[Suppression of frameshift mutation as a result of partial inactivation of translation termination factors in Saccharomyces cerevisiae yeast].

V N Kulikov1, O N Tikhodeev, F S Forafonov, A S Borkhsenius, V V Alenin, S G Inge-Vechtomov.   

Abstract

Special search for frameshift mutations, which are suppressed by the cytoplasmic [PSI] factor and by omnipotent nonsense suppressors (recessive mutations in the SUP35 and SUP45 genes), partially inactivating a translation termination complex, was initiated in the LYS2 gene in the yeast Saccharomyces cerevisiae. Mutations were obtained after exposure to UV light and treatment with a mixture consisting of 1.6- and 1.8-dinitropyrene (DNP). This mixture was shown to induce mutations of the frameshift type with a high frequency. The majority of these mutations were insertions of one A or T, which is in good agreement with the data obtained in studies of DNP-induced mutagenesis in other eukaryotes. Frameshift suppression in yeast was first shown on the example of the mutation obtained in this work (lys2-90), which carried the insertion of an extra T in the sequence of five T. This frameshift suppression was shown to occur in the presence of the [PSI] factor (i.e., due to the prion form of the translation release factor eRF3) and as a result of mutations in genes SUP35 or SUP45, which partially inactivate translation termination factors eRF3 and eRF1, respectively. Alternative mechanisms of programmed translational frameshifting in the course of translation and the possibility of enhancing the effectiveness of such frameshifting in the presence of the [PSI] factor are considered.

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Year:  2001        PMID: 11436550

Source DB:  PubMed          Journal:  Genetika        ISSN: 0016-6758


  1 in total

1.  [PIN (+)]-dependent induction of protease-resistant amyloids by Ade2p protein fused with prionizing NM domain of Sup35 protein of the yeast Saccharomyces cerevisiae.

Authors:  A A Pogoda; V V Alenin; A S Borchsenius; S P Zadorsky; V V Manukhov; S G Inge-Vechtomov
Journal:  Dokl Biochem Biophys       Date:  2010-08-17       Impact factor: 0.788

  1 in total

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