Structure of tRNA splicing enzyme Tpt1 illuminates the mechanism of RNA 2′-PO4 recognition and ADP-ribosylation

Ankan Banerjee; Annum Munir; Leonora Abdullahu; Masad J. Damha; Yehuda Goldgur; Stewart Shuman

doi:10.1038/s41467-018-08211-9

Nature Communications (Jan 2019)

Structure of tRNA splicing enzyme Tpt1 illuminates the mechanism of RNA 2′-PO4 recognition and ADP-ribosylation

Ankan Banerjee,
Annum Munir,
Leonora Abdullahu,
Masad J. Damha,
Yehuda Goldgur,
Stewart Shuman

Affiliations

Ankan Banerjee: Molecular Biology and Structural Biology Programs, Sloan-Kettering Institute
Annum Munir: Molecular Biology and Structural Biology Programs, Sloan-Kettering Institute
Leonora Abdullahu: Chemistry Department, McGill University
Masad J. Damha: Chemistry Department, McGill University
Yehuda Goldgur: Molecular Biology and Structural Biology Programs, Sloan-Kettering Institute
Stewart Shuman: Molecular Biology and Structural Biology Programs, Sloan-Kettering Institute

DOI: https://doi.org/10.1038/s41467-018-08211-9
Journal volume & issue: Vol. 10, no. 1
pp. 1 – 10

Abstract

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Tpt1 catalyzes the final essential step in yeast tRNA splicing and is a potential antifungal target. Here the authors provide structural insights into how Tpt1 recognizes a 2’-PO4 RNA splice junction and the mechanism of RNA phospho-ADP-ribosylation.

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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