Mechanism of aminoacyl-tRNA acetylation by an aminoacyl-tRNA acetyltransferase AtaT from enterohemorrhagic E. coli

AtaT is a type-II toxin from enterohemorrhagic E. coli, reported to acetylate the aminoacyl-moiety of initiator Met-tRNAfMet, thus inhibiting translation initiation. Biochemical analysis suggests that AtaT has a broader specificity for aminoacyl-tRNAs and inhibits global translation. Structure of At...

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Autores principales:	Yuka Yashiro, Yuriko Sakaguchi, Tsutomu Suzuki, Kozo Tomita
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/b756a25d8bce42908de151680c466bc3
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spelling	oai:doaj.org-article:b756a25d8bce42908de151680c466bc32021-12-02T17:33:12ZMechanism of aminoacyl-tRNA acetylation by an aminoacyl-tRNA acetyltransferase AtaT from enterohemorrhagic E. coli10.1038/s41467-020-19281-z2041-1723https://doaj.org/article/b756a25d8bce42908de151680c466bc32020-10-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-19281-zhttps://doaj.org/toc/2041-1723AtaT is a type-II toxin from enterohemorrhagic E. coli, reported to acetylate the aminoacyl-moiety of initiator Met-tRNAfMet, thus inhibiting translation initiation. Biochemical analysis suggests that AtaT has a broader specificity for aminoacyl-tRNAs and inhibits global translation. Structure of AtaT in complex with acetylated Met-tRNAfMet offers insight into the substrate selection by the enzyme.Yuka YashiroYuriko SakaguchiTsutomu SuzukiKozo TomitaNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-12 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Yuka Yashiro Yuriko Sakaguchi Tsutomu Suzuki Kozo Tomita Mechanism of aminoacyl-tRNA acetylation by an aminoacyl-tRNA acetyltransferase AtaT from enterohemorrhagic E. coli
description	AtaT is a type-II toxin from enterohemorrhagic E. coli, reported to acetylate the aminoacyl-moiety of initiator Met-tRNAfMet, thus inhibiting translation initiation. Biochemical analysis suggests that AtaT has a broader specificity for aminoacyl-tRNAs and inhibits global translation. Structure of AtaT in complex with acetylated Met-tRNAfMet offers insight into the substrate selection by the enzyme.
format	article
author	Yuka Yashiro Yuriko Sakaguchi Tsutomu Suzuki Kozo Tomita
author_facet	Yuka Yashiro Yuriko Sakaguchi Tsutomu Suzuki Kozo Tomita
author_sort	Yuka Yashiro
title	Mechanism of aminoacyl-tRNA acetylation by an aminoacyl-tRNA acetyltransferase AtaT from enterohemorrhagic E. coli
title_short	Mechanism of aminoacyl-tRNA acetylation by an aminoacyl-tRNA acetyltransferase AtaT from enterohemorrhagic E. coli
title_full	Mechanism of aminoacyl-tRNA acetylation by an aminoacyl-tRNA acetyltransferase AtaT from enterohemorrhagic E. coli
title_fullStr	Mechanism of aminoacyl-tRNA acetylation by an aminoacyl-tRNA acetyltransferase AtaT from enterohemorrhagic E. coli
title_full_unstemmed	Mechanism of aminoacyl-tRNA acetylation by an aminoacyl-tRNA acetyltransferase AtaT from enterohemorrhagic E. coli
title_sort	mechanism of aminoacyl-trna acetylation by an aminoacyl-trna acetyltransferase atat from enterohemorrhagic e. coli
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/b756a25d8bce42908de151680c466bc3
work_keys_str_mv	AT yukayashiro mechanismofaminoacyltrnaacetylationbyanaminoacyltrnaacetyltransferaseatatfromenterohemorrhagicecoli AT yurikosakaguchi mechanismofaminoacyltrnaacetylationbyanaminoacyltrnaacetyltransferaseatatfromenterohemorrhagicecoli AT tsutomusuzuki mechanismofaminoacyltrnaacetylationbyanaminoacyltrnaacetyltransferaseatatfromenterohemorrhagicecoli AT kozotomita mechanismofaminoacyltrnaacetylationbyanaminoacyltrnaacetyltransferaseatatfromenterohemorrhagicecoli
_version_	1718380021888843776

Mechanism of aminoacyl-tRNA acetylation by an aminoacyl-tRNA acetyltransferase AtaT from enterohemorrhagic E. coli

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