Differential transcription of the two Saccharomyces cerevisiae genes encoding elongation factor 2

Veldman, Sarah A.; Rao, Sulekha; Bodley, James W.

doi:10.1016/0378-1119(94)90248-8

Cited by 6 publications

(5 citation statements)

References 11 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Among non‐Elongator factors able to contact Kti11p are 40S ribosomal proteins, Rps7Ap and Rps19Ap (Fig. 3B) (Baker et al ., 1996; Planta and Mager, 1998), and other translational factors: translation elongation factor 2 (EF2), Eft2p (Veldman et al ., 1994), Dph2p involved in diphthamide synthesis and Eft2p function (Mattheakis et al ., 1993) and Yil103wp, a product, consistent with our TAP approach, reported to interact with Dph2p by two‐hybrid analysis (Ito et al ., 2001) (Fig. 3B).…”

Section: Resultsmentioning

confidence: 99%

Elongator's toxin‐target (TOT) function is nuclear localization sequence dependent and suppressed by post‐translational modification

Fichtner

Jablonowski

Schierhorn

et al. 2003

Molecular Microbiology

124

View full text Add to dashboard Cite

SummaryThe toxin target (TOT) function of the Saccharomyces cerevisiae Elongator complex enables Kluyveromyces lactis zymocin to induce a G1 cell cycle arrest. Loss of a ubiquitin-related system ( URM1-UBA4 ) and KTI11 enhances post-translational modification/proteolysis of Elongator subunit Tot1p (Elp1p) and abrogates its TOT function. Using TAP tagging, Kti11p contacts Elongator and translational proteins (Rps7Ap, Rps19Ap Eft2p, Yil103wp, Dph2p). Loss of YIL103w and DPH2 (involved in diphtheria toxicity) suppresses zymocicity implying that both toxins overlap in a manner mediated by Kti11p. Among the pool that co-fractionates with RNA polymerase II (pol II) and nucleolin, Nop1p, unmodified Tot1p dominates. Thus, modification/proteolysis may affect association of Elongator with pol II or its localization. Consistently, an Elongator-nuclear localization sequence (NLS) targets green fluorescent protein (GFP) to the nucleus, and its truncation yields TOT deficiency. Similarly, KAP120 deletion rescues cells from zymocin, suggesting that Elongator's TOT function requires NLS-and karyopherin-dependent nuclear import.

show abstract

Section: Resultsmentioning

confidence: 99%

Elongator's toxin‐target (TOT) function is nuclear localization sequence dependent and suppressed by post‐translational modification

Fichtner

Jablonowski

Schierhorn

et al. 2003

Molecular Microbiology

124

View full text Add to dashboard Cite

show abstract

“…It is noteworthy that 21 spontaneous mutants with changes on EFT2 were found but that none had mutations on EFT1. This may be due to the partial dominance of the resistant phenotype and the fact that the EFT2 promoter seems to be 2.5-fold more active than that of EFT1 (24). A highly dominant phenotype may be needed to detect EFT1 mutants when EFT2 is being expressed at such high levels.…”

Section: Discussionmentioning

confidence: 99%

“…This is an available labeled analog of GM193663 which competes for binding and shows cross-resistance (data not shown). A background of binding activity was expected, and indeed was observed, due to the presence of the EF2 protein expressed from the EFT1 gene, the second gene encoding EF2 in S. cerevisiae (21,24). To simplify the system, EFT1 was interrupted in eight resistant strains with unique mutations in EF2.…”

Section: Gm193663-resistant Mutants Fall Into Two Complementation Gromentioning

confidence: 99%

Translation Elongation Factor 2 Is Part of the Target for a New Family of Antifungals

Capa

Mendoza

Lavandera

et al. 1998

Antimicrob Agents Chemother

View full text Add to dashboard Cite

Translation elongation factor 2 (EF2), which in Saccharomyces cerevisiae is expressed from the EFT1 andEFT2 genes, has been found to be targeted by a new family of highly specific antifungal compounds derived from the natural product sordarin. Two complementation groups of mutants resistant to the semisynthetic sordarin derivative GM193663 were found. The major one (21 members) consisted of isolates with mutations onEFT2. The minor one (four isolates) is currently being characterized but it is already known that resistance in this group is not due to mutations on EFT1, pointing to the complex structure of the functional target for these compounds. Mutations on EF2 clustered, forming a possible drug binding pocket on a three-dimensional model of EF2, and mutant cell extracts lost the capacity to bind to the inhibitors. This new family of antifungals holds the promise to be a much needed and potent addition to current antimicrobial treatments, as well as a useful tool for dissection of the elongation process in ribosomal protein synthesis.

show abstract

“…Notably, in yeast, the essential eEF2 protein is encoded by two genes, EFT1 and EFT2. Both genes encode identical proteins with EFT1 producing $30% and EFT2 $70% of the transcripts (Veldman et al, 1994). Deletion of either gene results in reduced eEF2 levels without an apparent growth defect (Murray et al, 2016) and the crystal structure of the S. cerevisiae eEF2 in complex with the anti-fungal compound Sordarin (PDB: 1N0U) (Jørgensen et al, 2003).…”

Section: Introductionmentioning

confidence: 99%

“…(legend continued on next page) (Perentesis et al, 1992;Veldman et al, 1994). While deletion of HGH1 does not impair growth (Rodriguez-Peñ a et al, 1998), deletion of both HGH1 and EFT2 causes a synthetic growth defect, suggesting a functional relation between eEF2 and Hgh1 (Costanzo et al, 2010).…”

Section: Introductionmentioning

confidence: 99%

Chaperone Function of Hgh1 in the Biogenesis of Eukaryotic Elongation Factor 2

et al. 2019

View full text Add to dashboard Cite

show abstract

Differential transcription of the two Saccharomyces cerevisiae genes encoding elongation factor 2

Cited by 6 publications

References 11 publications

Elongator's toxin‐target (TOT) function is nuclear localization sequence dependent and suppressed by post‐translational modification

Elongator's toxin‐target (TOT) function is nuclear localization sequence dependent and suppressed by post‐translational modification

Translation Elongation Factor 2 Is Part of the Target for a New Family of Antifungals

Chaperone Function of Hgh1 in the Biogenesis of Eukaryotic Elongation Factor 2

Contact Info

Product

Resources

About