title: Yeast alpha-tubulin suppressor Ats1/Kti13 relates to the Elongator complex and interacts with Elongator partner protein Kti11.
abstract: The alpha-tubulin suppressor 1 (ATS1) gene and the killer toxin-insensitive 13 (KTI13) locus from Saccharomyces cerevisiae are allelic. The Ats1/Kti13 gene product interacts with the cell polarity factor Nap1 and promotes growth inhibition of S. cerevisiae by zymocin, a tRNAse toxin complex from Kluyveromyces lactis. Kti13 removal causes zymocin resistance, a trait that is typical of defects in the Elongator complex. Here, we show that Kti13 co-purifies with the Elongator partner protein Kti11 and that the Kti11 interaction, not the Nap1 partnership, requires the C-terminus of Kti13. Moreover, Kti13 functionally relates to roles of the Elongator complex in tRNA wobble uridine modification, tRNA suppression of nonsense (SUP4) and missense (SOE1) mutations and tRNA restriction by zymocin. Also, inactivation of Kti13 or Elongator rescues the thermosensitive growth defect of secretory mutants (sec2-59(ts), sec12-4(ts)), suggesting that Kti13 and Elongator affect secretion processes that depend on the GTP exchange factors Sec2 and Sec12 respectively. Distinct from tandem deletions in KTI13 and Elongator genes, a kti13Delta kti11Delta double deletion induces synthetic sickness or lethality. In sum, our data suggest that Kti13 and Kti11 support Elongator functions and that they both share Elongator-independent role(s) that are important for cell viability.
authors.affiliation: Biologicum, Institut für Biologie, Institutsbereich Genetik, Martin-Luther-Universität, Halle-Wittenberg, Weinbergweg 10, D-06120 Halle (Saale), Germany.
authors.forename: René
authors.initials: R
authors.lastname: Zabel
authors.forename: Christian
authors.initials: C
authors.lastname: Bär
authors.forename: Constance
authors.initials: C
authors.lastname: Mehlgarten
authors.forename: Raffael
authors.initials: R
authors.lastname: Schaffrath
mesh_terms: D001692:Biological Transport; D018797:Cell Cycle Proteins / Q000235:genetics / Q000378:metabolism; D003593:Cytoplasm / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D015966:Gene Expression Regulation, Fungal; D055646:Killer Factors, Yeast; D007716:Kluyveromyces / Q000378:metabolism; D009154:Mutation; D009183:Mycotoxins / Q000494:pharmacology; D009687:Nuclear Proteins / Q000235:genetics / Q000378:metabolism; D056490:Nucleosome Assembly Protein 1; D010445:Peptide Elongation Factors / Q000235:genetics / Q000378:metabolism*; D011485:Protein Binding; D012343:RNA, Transfer / Q000378:metabolism; D012097:Repressor Proteins / Q000032:analysis / Q000235:genetics / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000737:chemistry / Q000187:drug effects / Q000235:genetics / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins / Q000032:analysis / Q000235:genetics / Q000378:metabolism*; D013489:Suppression, Genetic
chemical_list: C089099:ATS1 protein, S cerevisiae; D018797:Cell Cycle Proteins; C459979:KTI11 protein, S cerevisiae; D055646:Killer Factors, Yeast; D009183:Mycotoxins; C533556:NAP1 protein, S cerevisiae; D009687:Nuclear Proteins; D056490:Nucleosome Assembly Protein 1; D010445:Peptide Elongation Factors; D012097:Repressor Proteins; D029701:Saccharomyces cerevisiae Proteins; C058975:zymocin; D012343:RNA, Transfer