Crystal structure of the Lin28-interacting module of human terminal uridylyltransferase that regulates let-7 expression

Seisuke Yamashita; Takashi Nagaike; Kozo Tomita

doi:10.1038/s41467-019-09966-5

Nature Communications (Apr 2019)

Crystal structure of the Lin28-interacting module of human terminal uridylyltransferase that regulates let-7 expression

Seisuke Yamashita,
Takashi Nagaike,
Kozo Tomita

Affiliations

Seisuke Yamashita: Department of Computational Biology and Medical Sciences, Graduate School of Frontier Sciences, The University of Tokyo
Takashi Nagaike: Department of Computational Biology and Medical Sciences, Graduate School of Frontier Sciences, 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/s41467-019-09966-5
Journal volume & issue: Vol. 10, no. 1
pp. 1 – 11

Abstract

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Terminal uridylyltransferase 4/7 (TUT4/7) binds to Lin28 and modifies let-7 precursor (pre-let-7) to regulate cell differentiation and proliferation. Here the authors report the crystal structure of the N-terminal Lin28-interacting module of TUT4, showing a role of the N-terminal zinc finger domain in stabilizing the Lin28:pre-let-7:TUT4 ternary complex.

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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