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

Yuka Yashiro; Yuriko Sakaguchi; Tsutomu Suzuki; Kozo Tomita

doi:10.1038/s41467-020-19281-z

Nature Communications (Oct 2020)

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

Yuka Yashiro,
Yuriko Sakaguchi,
Tsutomu Suzuki,
Kozo Tomita

Affiliations

Yuka Yashiro: Department of Computational Biology and Medical Sciences, Graduate School of Frontier Sciences, The University of Tokyo
Yuriko Sakaguchi: Department of Chemistry and Biotechnology, Graduate School of Engineering, The University of Tokyo
Tsutomu Suzuki: Department of Chemistry and Biotechnology, Graduate School of Engineering, The University of Tokyo
Kozo Tomita: Department of Computational Biology and Medical Sciences, Graduate School of Frontier Sciences, The University of Tokyo

DOI: https://doi.org/10.1038/s41467-020-19281-z
Journal volume & issue: Vol. 11, no. 1
pp. 1 – 12

Abstract

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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.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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