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Charlotte Rohde Knudsen

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

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Aminoacyl-tRNA-charged eukaryotic elongation factor 1A is a bona fide substrate for Legionelle pneumophila effector glucosyltransferases. / Tzivelekidis, Tina; Jank, Thomas; Pohl, Corinna; Schlosser, Andreas; Rospert, Sabine; Knudsen, Charlotte Rohde; Rodnina, Marina; Belyi, Yuri; Aktories, Klaus.

I: P L o S One, Bind 6, Nr. 12, 22.12.2011, s. e29525.

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review

Harvard

Tzivelekidis, T, Jank, T, Pohl, C, Schlosser, A, Rospert, S, Knudsen, CR, Rodnina, M, Belyi, Y & Aktories, K 2011, 'Aminoacyl-tRNA-charged eukaryotic elongation factor 1A is a bona fide substrate for Legionelle pneumophila effector glucosyltransferases' P L o S One, bind 6, nr. 12, s. e29525. https://doi.org/10.1371/journal.pone.0029525

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Author

Tzivelekidis, Tina ; Jank, Thomas ; Pohl, Corinna ; Schlosser, Andreas ; Rospert, Sabine ; Knudsen, Charlotte Rohde ; Rodnina, Marina ; Belyi, Yuri ; Aktories, Klaus. / Aminoacyl-tRNA-charged eukaryotic elongation factor 1A is a bona fide substrate for Legionelle pneumophila effector glucosyltransferases. I: P L o S One. 2011 ; Bind 6, Nr. 12. s. e29525.

Bibtex

@article{d21ac6d505054994a70ff42e973b1283,
title = "Aminoacyl-tRNA-charged eukaryotic elongation factor 1A is a bona fide substrate for Legionelle pneumophila effector glucosyltransferases",
abstract = "Legionella pneumophila, which is the causative organism of Legionnaires 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 Lgtcatalyzed 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.",
author = "Tina Tzivelekidis and Thomas Jank and Corinna Pohl and Andreas Schlosser and Sabine Rospert and Knudsen, {Charlotte Rohde} and Marina Rodnina and Yuri Belyi and Klaus Aktories",
year = "2011",
month = "12",
day = "22",
doi = "10.1371/journal.pone.0029525",
language = "English",
volume = "6",
pages = "e29525",
journal = "P L o S One",
issn = "1932-6203",
publisher = "public library of science",
number = "12",

}

RIS

TY - JOUR

T1 - Aminoacyl-tRNA-charged eukaryotic elongation factor 1A is a bona fide substrate for Legionelle pneumophila effector glucosyltransferases

AU - Tzivelekidis, Tina

AU - Jank, Thomas

AU - Pohl, Corinna

AU - Schlosser, Andreas

AU - Rospert, Sabine

AU - Knudsen, Charlotte Rohde

AU - Rodnina, Marina

AU - Belyi, Yuri

AU - Aktories, Klaus

PY - 2011/12/22

Y1 - 2011/12/22

N2 - Legionella pneumophila, which is the causative organism of Legionnaires 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 Lgtcatalyzed 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.

AB - Legionella pneumophila, which is the causative organism of Legionnaires 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 Lgtcatalyzed 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.

U2 - 10.1371/journal.pone.0029525

DO - 10.1371/journal.pone.0029525

M3 - Journal article

VL - 6

SP - e29525

JO - P L o S One

JF - P L o S One

SN - 1932-6203

IS - 12

ER -