Rodnina, Marina V.

[["dc.bibliographiccitation.firstpage","35629"],["dc.bibliographiccitation.issue","49"],["dc.bibliographiccitation.journal","Journal of biological chemistry"],["dc.bibliographiccitation.lastpage","35637"],["dc.bibliographiccitation.volume","282"],["dc.contributor.author","Gromadski, Kirill B."],["dc.contributor.author","Schuemmer, Tobias"],["dc.contributor.author","Stromgaard, Anne"],["dc.contributor.author","Knudsen, Charlotte R."],["dc.contributor.author","Kinzy, Terri Goss"],["dc.contributor.author","Rodnina, Marina"],["dc.date.accessioned","2017-09-07T11:49:21Z"],["dc.date.available","2017-09-07T11:49:21Z"],["dc.date.issued","2007"],["dc.description.abstract","The interactions of elongation factor 1A (eEF1A) from Saccharomyces cerevisiae with elongation factor 1B alpha (eEF1B alpha), guanine nucleotides, and aminoacyl-tRNA were studied kinetically by fluorescence stopped-flow. eEF1A has similar affinities for GDP and GTP, 0.4 and 1.1 mu M, respectively. Dissociation of nucleotides from eEF1A in the absence of the guanine nucleotide exchange factor is slow ( about 0.1s(-1)) and is accelerated by eEF1B alpha by 320-fold and 250-fold for GDP and GTP, respectively. The rate constant of eEF1B alpha binding to eEF1A (10(7)-10(8) M-1 s(-1)) is independent of guanine nucleotides. At the concentrations of nucleotides and factors prevailing in the cell, the overall exchange rate is expected to be in the range of 6 s(-1), which is compatible with the rate of protein synthesis in the cell. eEF1A center dot GTP binds Phe-tRNA(Phe) with a K-d of 3 nM, whereas eEF1A center dot GDP shows no significant binding, indicating that eEF1A has similar tRNA binding properties as its prokaryotic homolog, EF-Tu."],["dc.identifier.doi","10.1074/jbc.M707245200"],["dc.identifier.gro","3143400"],["dc.identifier.isi","000251458100023"],["dc.identifier.pmid","17925388"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/910"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: NIGMS NIH HHS [R01 GM057483, R01 GM057483-10]"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Amer Soc Biochemistry Molecular Biology Inc"],["dc.relation.issn","0021-9258"],["dc.title","Kinetics of the interactions between yeast elongation factors 1A and 1B alpha, guanine nucleotides, and aminoacyl-tRNA"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","21139"],["dc.bibliographiccitation.issue","30"],["dc.bibliographiccitation.journal","Journal of biological chemistry"],["dc.bibliographiccitation.lastpage","21146"],["dc.bibliographiccitation.volume","281"],["dc.contributor.author","Dahl, Louise D."],["dc.contributor.author","Wieden, Hans-Joachim"],["dc.contributor.author","Rodnina, Marina"],["dc.contributor.author","Knudsen, Charlotte R."],["dc.date.accessioned","2017-09-07T11:52:39Z"],["dc.date.available","2017-09-07T11:52:39Z"],["dc.date.issued","2006"],["dc.description.abstract","Elongation factor Ts (EF-Ts) is the guanine nucleotide exchange factor for elongation factor Tu (EF-Tu). An important feature of the nucleotide exchange is the structural rearrangement of EF-Tu in the EF-Tu.EF-Ts complex caused by insertion of Phe-81 of EF-Ts between His-84 and His-118 of EF-Tu. In this study, the contribution of His-118 to nucleotide release was studied by pre-steady state kinetic analysis of nucleotide exchange in EF-Tu mutants in which His-118 was replaced by Ala or Glu. Intrinsic as well as EF-Ts-catalyzed release of GDP/ GTP was affected by the mutations, resulting in an similar to 10-fold faster spontaneous nucleotide release and a 10-50-fold slower EF-Ts-catalyzed nucleotide release. The effects are attributed to the interference of the mutations with the EF-Ts-induced movements of the P-loop of EF-Tu and changes at the domain 1/3 interface, leading to the release of the beta-phosphate group of GTP/GDP. The K-d for GTP is increased by more than 40 times when His-118 is replaced with Glu, which may explain the inhibition by His-118 mutations of aminoacyl-tRNA binding to EF-Tu. The mutations had no effect on EF-Tu-dependent delivery of aminoacyl-tRNA to the ribosome."],["dc.identifier.doi","10.1074/jbc.M602068200"],["dc.identifier.gro","3143653"],["dc.identifier.isi","000239187300050"],["dc.identifier.pmid","16717093"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1191"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Amer Soc Biochemistry Molecular Biology Inc"],["dc.relation.eissn","1083-351X"],["dc.relation.issn","0021-9258"],["dc.title","The importance of P-loop and domain movements in EF-Tu for guanine nucleotide exchange"],["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"]]