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SSD1 modifies phenotypes of Elongator mutants
Umeå University, Faculty of Science and Technology, Department of Molecular Biology (Faculty of Science and Technology).ORCID iD: 0000-0003-3299-6415
Umeå University, Faculty of Medicine, Department of Molecular Biology (Faculty of Medicine).
Umeå University, Faculty of Medicine, Department of Odontology.
2019 (English)In: Current Genetics, ISSN 0172-8083, E-ISSN 1432-0983Article in journal (Refereed) Epub ahead of print
Abstract [en]

The translational decoding properties of tRNAs are influenced by post-transcriptional modification of nucleosides in their anticodon region. The Elongator complex promotes the first step in the formation of 5-methoxycarbonylmethyl (mcm(5)), 5-methoxycarbonylhydroxymethyl (mchm(5)), and 5-carbamoylmethyl (ncm(5)) groups on wobble uridine residues in eukaryotic cytosolic tRNAs. Elongator mutants in yeast, worms, plants, mice, and humans not only show a tRNA modification defect, but also a diverse range of additional phenotypes. Even though the phenotypes are almost certainly caused by the reduced functionality of the hypomodified tRNAs in translation, the basis for specific phenotypes is not well understood. Here, we discuss the recent finding that the phenotypes of Saccharomyces cerevisiae Elongator mutants are modulated by the genetic background. This background-effect is largely due to the allelic variation at the SSD1 locus, which encodes an mRNA-binding protein involved in post-transcriptional regulation of gene expression. A nonsense ssd1 allele is found in several wild-type laboratory strains and the presence of this allele aggravates the stress-induced phenotypes of Elongator mutants. Moreover, other phenotypes, such as the histone acetylation and telomeric gene silencing defects, are dependent on the mutant ssd1 allele. Thus, SSD1 is a genetic modifier of the phenotypes of Elongator-deficient yeast cells.

Place, publisher, year, edition, pages
Springer-Verlag New York, 2019.
Keywords [en]
Elongator complex, tRNA modification, Translation, mRNA-binding protein
National Category
Biochemistry and Molecular Biology Genetics
Identifiers
URN: urn:nbn:se:umu:diva-166507DOI: 10.1007/s00294-019-01048-9ISI: 000498973600001PubMedID: 31776648OAI: oai:DiVA.org:umu-166507DiVA, id: diva2:1380115
Available from: 2019-12-18 Created: 2019-12-18 Last updated: 2019-12-18

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Xu, FuByström, AndersJohansson, Marcus J. O.

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Department of Molecular Biology (Faculty of Science and Technology)Department of Molecular Biology (Faculty of Medicine)Department of Odontology
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