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Crystal structures of U6 snRNA-specific terminal uridylyltransferase

After transcription the 3′-end of U6 snRNA is oligo-uridylylated by the terminal uridylyltransferase TUT1. Here the authors present the crystal structure of human TUT1 and give insights into the mechanism of 3′-end uridylylation by the enzyme.

Seisuke Yamashita
Yuko Takagi
Kozo Tomita
ResearchOpen Access07 Jun 2017
Nature Communications

Volume: 8, P: 1-11
Mechanism of U6 snRNA oligouridylation by human TUT1

U6 snRNA plays a catalytic role in pre-mRNA splicing. Here the authors report the structure of human terminal uridyltransferase, TUT1, complexed with U6 snRNA revealing the mechanism of specific uridylation of U6 snRNA by TUT1.

Seisuke Yamashita
Kozo Tomita
ResearchOpen Access10 Aug 2023
Nature Communications

Volume: 14, P: 1-10
Crystal structure of the Lin28-interacting module of human terminal uridylyltransferase that regulates let-7 expression

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.

Seisuke Yamashita
Takashi Nagaike
Kozo Tomita
ResearchOpen Access29 Apr 2019
Nature Communications

Volume: 10, P: 1-11
Controlling exfoliation in order to minimize damage during dispersion of long SWCNTs for advanced composites

Howon Yoon
Motoi Yamashita
Kenji Hata
ResearchOpen Access28 Jan 2014
Scientific Reports

Volume: 4, P: 1-8
Reversible RNA phosphorylation stabilizes tRNA for cellular thermotolerance

Reversible internal RNA phosphrylation contributes to thermal stability and nuclease resistance of tRNA, and cellular thermotolerance of hyperthermophiles.

Takayuki Ohira
Keiichi Minowa
Tsutomu Suzuki
ResearchOpen Access27 Apr 2022
Nature

Volume: 605, P: 372-379
Acetate-dependent tRNA acetylation required for decoding fidelity in protein synthesis

A comparative genomic approach identified a novel acetate-dependent tRNA-modifying enzyme that catalyzes RNA acetylation with a mechanism similar to tRNA aminoacylation. This modification maintains decoding fidelity in protein synthesis.

Takaaki Taniguchi
Kenjyo Miyauchi
Tsutomu Suzuki
Research27 Aug 2018
Nature Chemical Biology

Volume: 14, P: 1010-1020

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Crystal structures of U6 snRNA-specific terminal uridylyltransferase

Mechanism of U6 snRNA oligouridylation by human TUT1

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

Controlling exfoliation in order to minimize damage during dispersion of long SWCNTs for advanced composites

Reversible RNA phosphorylation stabilizes tRNA for cellular thermotolerance

Acetate-dependent tRNA acetylation required for decoding fidelity in protein synthesis

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