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

AI Article Synopsis

  • - The Elongator complex in *Saccharomyces cerevisiae* is crucial for allowing the zymocin toxin from *Kluyveromyces lactis* to cause a G1 cell cycle arrest, with its function dependent on the presence of a ubiquitin-related system.
  • - Specific proteins, like Kti11p, interact with Elongator and proteins involved in translation, while the loss of certain genes (YIL103w and DPH2) reduces the impact of zymocin toxicity, suggesting overlapping mechanisms between different toxins.
  • - Proper localization of the Elongator complex to the nucleus is vital for its function, as demonstrated by experiments showing that modifications affecting its proteins can hinder its association with

Article Abstract

The 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.

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Source
http://dx.doi.org/10.1046/j.1365-2958.2003.03632.xDOI Listing

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