Aminoacyl-tRNA-charged eukaryotic elongation factor 1A is the bona fide substrate for Legionella pneumophila effector glucosyltransferases

Abstract: Legionella pneumophila, which is the causative organism of Legionnaireś disease, translocates numerous effector proteins into the host cell cytosol by a type IV secretion system during infection. Among the most potent effector proteins of Legionella are glucosyltransferases (lgt's), which selectively modify eukaryotic elongation factor (eEF) 1A at Ser-53 in the GTP binding domain. Glucosylation results in inhibition of protein synthesis. Here we show that in vitro glucosylation of yeast and mouse eEF1A by Lgt3 in the presence of the factors Phe-tRNAPhe and GTP was enhanced 150 and 590-fold, respectively. The glucosylation of eEF1A catalyzed by Lgt1 and 2 was increased about 70-fold. By comparison of uncharged tRNA with two distinct aminoacyl-tRNAs (His-tRNAHis and Phe-tRNAPhe) we could show that aminoacylation is crucial for Lgt-catalyzed glucosylation. Aminoacyl-tRNA had no effect on the enzymatic properties of lgt's and did not enhance the glucosylation rate of eEF1A truncation mutants, consisting of the GTPase domain only or of a 5 kDa peptide covering Ser-53 of eEF1A. Furthermore, binding of aminoacyl-tRNA to eEF1A was not altered by glucosylation. Taken together, our data suggest that the ternary complex, consisting of eEF1A, aminoacyl-tRNA and GTP, is the bona fide substrate for lgt's

Angaben zum Objekt

• Standort: Deutsche Nationalbibliothek Frankfurt am Main
• Umfang: Online-Ressource
• Sprache: Englisch
• Anmerkungen: PLoS ONE. 6, 12 (2011), e29525, DOI 10.1371/journal.pone.0029525, issn: 1932-6203 ; IN COPYRIGHT http://rightsstatements.org/page/InC/1.0 rs

Klassifikation und Themen

• Klassifikation: Biowissenschaften, Biologie

Beteiligte, Orts- und Zeitangaben

• Ereignis: Veröffentlichung
• (wo): Freiburg
• (wer): Universität
• (wann): 2011
• Urheber: Tzivelekidis, Tina ; Jank, Thomas ; Pohl, Corinna ; Schlosser, Andreas ; Rospert, Sabine ; Aktories, Klaus
• Beteiligte Personen und Organisationen: Institut für Experimentelle und Klinische Pharmakologie und Toxikologie ; Albert-Ludwigs-Universität Freiburg ; Zentrum für Biosystemanalyse ; Medizinische Fakultät ; Institut für Biochemie und Molekularbiologie

Weitere Informationen

• DOI: 10.1371/journal.pone.0029525
• URN: urn:nbn:de:bsz:25-freidok-118490
• Rechteinformation: Der Zugriff auf das Objekt ist unbeschränkt möglich.
• Letzte Aktualisierung: 25.03.2025, 13:46 MEZ