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Subunit communications crucial for the functional integrity of the yeast RNA polymerase II elongator (gamma-toxin target (TOT)) complex. | LitMetric

AI Article Synopsis

  • The study examines how the Elongator complex in yeast (Saccharomyces cerevisiae) aids in preventing cell cycle progression when exposed to the Kluyveromyces lactis zymocin through the gamma-toxin target (TOT) function.
  • Key subunits of the Elongator complex, especially Tot1p (Elp1p), are crucial for the structural integrity and protein interactions within Elongator, impacting the functions of other subunits like Tot2p (Elp2p) and Tot5p (Elp5p).
  • The research also highlights that the interactions between Elongator and various proteins require preassembled complexes and specific gene functions, suggesting a complex regulatory mechanism that links Elong

Article Abstract

In response to the Kluyveromyces lactis zymocin, the gamma-toxin target (TOT) function of the Saccharomyces cerevisiae RNA polymerase II (pol II) Elongator complex prevents sensitive strains from cell cycle progression. Studying Elongator subunit communications, Tot1p (Elp1p), the yeast homologue of human IKK-associated protein, was found to be essentially involved in maintaining the structural integrity of Elongator. Thus, the ability of Tot2p (Elp2p) to interact with the HAT subunit Tot3p (Elp3p) of Elongator and with subunit Tot5p (Elp5p) is dependent on Tot1p (Elp1p). Also, the association of core-Elongator (Tot1-3p/Elp1-3p) with HAP (Elp4-6p/Tot5-7p), the second three-subunit subcomplex of Elongator, was found to be sensitive to loss of TOT1 (ELP1) gene function. Structural integrity of the HAP complex itself requires the ELP4/TOT7, ELP5/TOT5, and ELP6/TOT6 genes, and elp6Delta/tot6Delta as well as elp4Delta/tot7Delta cells can no longer promote interaction between Tot5p (Elp5p) and Tot2p (Elp2p). The association between Elongator and Tot4p (Kti12p), a factor that may modulate the TOT activity of Elongator, requires Tot1-3p (Elp1-3p) and Tot5p (Elp5p), indicating that this contact requires a preassembled holo-Elongator complex. Tot4p also binds pol II hyperphosphorylated at its C-terminal domain Ser(5) raising the possibility that Tot4p bridges the contact between Elongator and pol II.

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Source
http://dx.doi.org/10.1074/jbc.M210060200DOI Listing

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