Open Access
Nucleic Acids Research, volume 46, issue 15, pages 7873-7885
Escherichia coli ItaT is a type II toxin that inhibits translation by acetylating isoleucyl-tRNAIle
Wilcox Brendan
1
,
Osterman Ilya A
1, 2
,
Serebryakova M. V.
1, 2
,
Lukyanov Dmitry
2
,
Komarova Ekaterina S
1, 2
,
Gollan Bridget
3
,
Morozova Natalia
1, 4
,
Wolf Yuri I.
5
,
Makarova Kira S.
5
,
Helaine Sophie
3
,
Sergiev Petr V.
1, 2
,
Dubiley Svetlana
1, 6
,
Borukhov S.
7
,
Severinov Konstantin
1, 6, 8
1
5
National Center for Biotechnology Information, National Library of Medicine, Bethesda, MD 20894, USA
|
7
Department of Cell Biology, Rowan University School of Osteopathic Medicine at Stratford, Stratford, NJ 08084-1489, USA
|
8
Waksman Institute for Microbiology, Rutgers, The State University of New Jersey, Piscataway, NJ 08854, USA
|
Publication type: Journal Article
Publication date: 2018-06-21
Journal:
Nucleic Acids Research
Quartile SCImago
Q1
Quartile WOS
Q1
Impact factor: 14.9
ISSN: 03051048, 13624962
PubMed ID:
29931259
Genetics
Abstract
Abstract Prokaryotic toxin–antitoxin (TA) modules are highly abundant and are involved in stress response and drug tolerance. The most common type II TA modules consist of two interacting proteins. The type II toxins are diverse enzymes targeting various essential intracellular targets. The antitoxin binds to cognate toxin and inhibits its function. Recently, TA modules whose toxins are GNAT-family acetyltransferases were described. For two such systems, the target of acetylation was shown to be aminoacyl-tRNA: the TacT toxin targets aminoacylated elongator tRNAs, while AtaT targets the amino acid moiety of initiating tRNAMet. We show that the itaRT gene pair from Escherichia coli encodes a TA module with acetyltransferase toxin ItaT that specifically and exclusively acetylates Ile-tRNAIle thereby blocking translation and inhibiting cell growth. ItaT forms a tight complex with the ItaR antitoxin, which represses the transcription of itaRT operon. A comprehensive bioinformatics survey of GNAT acetyltransferases reveals that enzymes encoded by validated or putative TA modules are common and form a distinct branch of the GNAT family tree. We speculate that further functional analysis of such TA modules will result in identification of enzymes capable of specifically targeting many, perhaps all, aminoacyl tRNAs.
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- We do not take into account publications that without a DOI.
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- Statistics recalculated weekly.
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Wilcox B. et al. Escherichia coli ItaT is a type II toxin that inhibits translation by acetylating isoleucyl-tRNAIle // Nucleic Acids Research. 2018. Vol. 46. No. 15. pp. 7873-7885.
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Wilcox B., Osterman I. A., Serebryakova M. V., Lukyanov D., Komarova E. S., Gollan B., Morozova N., Wolf Y. I., Makarova K. S., Helaine S., Sergiev P. V., Dubiley S., Borukhov S., Severinov K. Escherichia coli ItaT is a type II toxin that inhibits translation by acetylating isoleucyl-tRNAIle // Nucleic Acids Research. 2018. Vol. 46. No. 15. pp. 7873-7885.
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TY - JOUR
DO - 10.1093/nar/gky560
UR - https://doi.org/10.1093%2Fnar%2Fgky560
TI - Escherichia coli ItaT is a type II toxin that inhibits translation by acetylating isoleucyl-tRNAIle
T2 - Nucleic Acids Research
AU - Wilcox, Brendan
AU - Lukyanov, Dmitry
AU - Gollan, Bridget
AU - Morozova, Natalia
AU - Osterman, Ilya A
AU - Serebryakova, M. V.
AU - Komarova, Ekaterina S
AU - Wolf, Yuri I.
AU - Makarova, Kira S.
AU - Helaine, Sophie
AU - Sergiev, Petr V.
AU - Dubiley, Svetlana
AU - Borukhov, S.
AU - Severinov, Konstantin
PY - 2018
DA - 2018/06/21 00:00:00
PB - Oxford University Press
SP - 7873-7885
IS - 15
VL - 46
PMID - 29931259
SN - 0305-1048
SN - 1362-4962
ER -
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@article{2018_Wilcox,
author = {Brendan Wilcox and Dmitry Lukyanov and Bridget Gollan and Natalia Morozova and Ilya A Osterman and M. V. Serebryakova and Ekaterina S Komarova and Yuri I. Wolf and Kira S. Makarova and Sophie Helaine and Petr V. Sergiev and Svetlana Dubiley and S. Borukhov and Konstantin Severinov},
title = {Escherichia coli ItaT is a type II toxin that inhibits translation by acetylating isoleucyl-tRNAIle},
journal = {Nucleic Acids Research},
year = {2018},
volume = {46},
publisher = {Oxford University Press},
month = {jun},
url = {https://doi.org/10.1093%2Fnar%2Fgky560},
number = {15},
pages = {7873--7885},
doi = {10.1093/nar/gky560}
}
Cite this
MLA
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Wilcox, Brendan, et al. “Escherichia coli ItaT is a type II toxin that inhibits translation by acetylating isoleucyl-tRNAIle.” Nucleic Acids Research, vol. 46, no. 15, Jun. 2018, pp. 7873-7885. https://doi.org/10.1093%2Fnar%2Fgky560.