Rodnina, Marina V.

[["dc.bibliographiccitation.firstpage","4894"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","Applied and Environmental Microbiology"],["dc.bibliographiccitation.lastpage","4899"],["dc.bibliographiccitation.volume","68"],["dc.contributor.author","Schirmer, J."],["dc.contributor.author","Wieden, Hans-Joachim"],["dc.contributor.author","Rodnina, Marina"],["dc.contributor.author","Aktories, Klaus"],["dc.date.accessioned","2017-09-07T11:45:16Z"],["dc.date.available","2017-09-07T11:45:16Z"],["dc.date.issued","2002"],["dc.description.abstract","The mosquitocidal toxin (MTX) produced by Bacillus sphaericus strain SSII-1 is an similar to97-kDa single-chain toxin which contains a 27-kDa enzyme domain harboring ADP-ribosyltransferase activity and a 70-kDa putative binding domain. Due to cytotoxicity toward bacterial cells, the 27-kDa enzyme fragment cannot be produced in Escherichia coli expression systems. However, a nontoxic 32-kDa N-terminal truncation of MTX can be expressed in E. coli and subsequently cleaved to an active 27-kDa enzyme fragment. In vitro the 27-kDa enzyme fragment of MTX ADP-ribosylated numerous proteins in E. coli lysates, with dominant labeling of an similar to45-kDa protein. Matrix-assisted laser desorption ionization-time-of-flight mass spectrometry combined with peptide mapping identified this protein as the E. coli elongation factor Tu (EF-Tu). ADP ribosylation of purified EF-Tu prevented the formation of the stable ternary EF-Tu (.) aminoacyl-tRNA (.) GTP complex, whereas the binding of GTP to EF-Tu was not altered. The inactivation of EF-Tu by MTX-mediated ADP-ribosylation and the resulting inhibition of bacterial protein synthesis are likely to play important roles in the cytotoxicity of the 27-kDa enzyme fragment of MTX toward E. coli."],["dc.identifier.doi","10.1128/AEM.68.10.4894-4899.2002"],["dc.identifier.gro","3144168"],["dc.identifier.isi","000178380900027"],["dc.identifier.pmid","12324336"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1762"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0099-2240"],["dc.title","Inactivation of the elongation factor Tu by mosquitocidal toxin-catalyzed mono-ADP-ribosylation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","e29525"],["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","PLOS ONE"],["dc.bibliographiccitation.volume","6"],["dc.contributor.author","Tzivelekidis, Tina"],["dc.contributor.author","Jank, Thomas"],["dc.contributor.author","Pohl, Corinna"],["dc.contributor.author","Schlosser, Andreas"],["dc.contributor.author","Rospert, Sabine"],["dc.contributor.author","Knudsen, Charlotte R."],["dc.contributor.author","Rodnina, Marina V."],["dc.contributor.author","Belyi, Yury"],["dc.contributor.author","Aktories, Klaus"],["dc.contributor.editor","Kwaik, Yousef Abu"],["dc.date.accessioned","2018-01-29T13:06:01Z"],["dc.date.available","2018-01-29T13:06:01Z"],["dc.date.issued","2011"],["dc.description.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-tRNA(Phe) 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-tRNA(His) and Phe-tRNA(Phe)) 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."],["dc.identifier.doi","10.1371/journal.pone.0029525"],["dc.identifier.pmid","22216304"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/11884"],["dc.language.iso","en"],["dc.notes.status","zu prüfen"],["dc.relation.eissn","1932-6203"],["dc.title","Aminoacyl-tRNA-charged eukaryotic elongation factor 1A is the bona fide substrate for Legionella pneumophila effector glucosyltransferases"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]