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Elongator's toxin-target (TOT) function is nuclear localization sequence dependent and suppressed by post-translational modification.
- Source :
-
Molecular microbiology [Mol Microbiol] 2003 Sep; Vol. 49 (5), pp. 1297-307. - Publication Year :
- 2003
-
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.
- Subjects :
- Active Transport, Cell Nucleus
Fungal Proteins genetics
Fungal Proteins metabolism
G1 Phase
Gene Deletion
Genes, Fungal
Genes, Reporter
Green Fluorescent Proteins
Histone Acetyltransferases
Karyopherins metabolism
Killer Factors, Yeast
Kluyveromyces metabolism
Luminescent Proteins genetics
Luminescent Proteins metabolism
Nuclear Proteins metabolism
Peptide Elongation Factors metabolism
Protein Interaction Mapping
Protein Processing, Post-Translational
RNA Polymerase II metabolism
Repressor Proteins genetics
Repressor Proteins metabolism
Ribonucleoproteins, Small Nucleolar metabolism
Saccharomyces cerevisiae genetics
Saccharomyces cerevisiae growth & development
Saccharomyces cerevisiae Proteins genetics
Saccharomyces cerevisiae Proteins metabolism
Mycotoxins metabolism
Nuclear Localization Signals metabolism
Saccharomyces cerevisiae metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0950-382X
- Volume :
- 49
- Issue :
- 5
- Database :
- MEDLINE
- Journal :
- Molecular microbiology
- Publication Type :
- Academic Journal
- Accession number :
- 12940988
- Full Text :
- https://doi.org/10.1046/j.1365-2958.2003.03632.x