Crystal structure of DmTailor in complex with U6 RNA

Kroupova, Alena; Ivascu, A.; Reimão-Pinto, Madalena M; Ameres, Stefan L.; Jínek, Martin

doi:10.2210/pdb6i0u/pdb

2018

DOI: 10.2210/pdb6i0u/pdb

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Crystal structure of DmTailor in complex with U6 RNA

Alena Kroupova

A. Ivascu

Madalena M Reimão-Pinto

et al.

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Cited by 5 publications

References 64 publications

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Functions and mechanisms of RNA tailing by metazoan terminal nucleotidyltransferases

Liudkovska

Dziembowski

2020

WIREs RNA

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Termini often determine the fate of RNA molecules. In recent years, 3′ ends of almost all classes of RNA species have been shown to acquire nontemplated nucleotides that are added by terminal nucleotidyltransferases (TENTs). The best‐described role of 3′ tailing is the bulk polyadenylation of messenger RNAs in the cell nucleus that is catalyzed by canonical poly(A) polymerases (PAPs). However, many other enzymes that add adenosines, uridines, or even more complex combinations of nucleotides have recently been described. This review focuses on metazoan TENTs, which are either noncanonical PAPs or terminal uridylyltransferases with varying processivity. These enzymes regulate RNA stability and RNA functions and are crucial in early development, gamete production, and somatic tissues. TENTs regulate gene expression at the posttranscriptional level, participate in the maturation of many transcripts, and protect cells against viral invasion and the transposition of repetitive sequences. This article is categorized under: RNA Interactions with Proteins and Other Molecules > Protein‐RNA Recognition RNA Processing > 3′ End Processing RNA Turnover and Surveillance > Regulation of RNA Stability

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Functions and mechanisms of RNA tailing by metazoan terminal nucleotidyltransferases

Liudkovska

Dziembowski

2020

WIREs RNA

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TENT2, TUT4, and TUT7 selectively regulate miRNA sequence and abundance

et al. 2022

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TENTs generate miRNA isoforms by 3’ tailing. However, little is known about how tailing regulates miRNA function. Here, we generate isogenic HEK293T cell lines in which TENT2, TUT4 and TUT7 are knocked out individually or in combination. Together with rescue experiments, we characterize TENT-specific effects by deep sequencing, Northern blot and in vitro assays. We find that 3’ tailing is not random but highly specific. In addition to its known adenylation, TENT2 contributes to guanylation and uridylation on mature miRNAs. TUT4 uridylates most miRNAs whereas TUT7 is dispensable. Removing adenylation has a marginal impact on miRNA levels. By contrast, abolishing uridylation leads to dysregulation of a set of miRNAs. Besides let-7, miR-181b and miR-222 are negatively regulated by TUT4/7 via distinct mechanisms while the miR-888 cluster is upregulated specifically by TUT7. Our results uncover the selective actions of TENTs in generating 3’ isomiRs and pave the way to investigate their functions.

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Structure and mechanism of CutA, RNA nucleotidyl transferase with an unusual preference for cytosine

Malik

Kobyłecki

Krawczyk

et al. 2020

Nucleic Acids Research

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Template-independent terminal ribonucleotide transferases (TENTs) catalyze the addition of nucleotide monophosphates to the 3′-end of RNA molecules regulating their fate. TENTs include poly(U) polymerases (PUPs) with a subgroup of 3′ CUCU-tagging enzymes, such as CutA in Aspergillus nidulans. CutA preferentially incorporates cytosines, processively polymerizes only adenosines and does not incorporate or extend guanosines. The basis of this peculiar specificity remains to be established. Here, we describe crystal structures of the catalytic core of CutA in complex with an incoming non-hydrolyzable CTP analog and an RNA with three adenosines, along with biochemical characterization of the enzyme. The binding of GTP or a primer with terminal guanosine is predicted to induce clashes between 2-NH2 of the guanine and protein, which would explain why CutA is unable to use these ligands as substrates. Processive adenosine polymerization likely results from the preferential binding of a primer ending with at least two adenosines. Intriguingly, we found that the affinities of CutA for the CTP and UTP are very similar and the structures did not reveal any apparent elements for specific NTP binding. Thus, the properties of CutA likely result from an interplay between several factors, which may include a conformational dynamic process of NTP recognition.

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Crystal structure of DmTailor in complex with U6 RNA

Cited by 5 publications

References 64 publications

Functions and mechanisms of RNA tailing by metazoan terminal nucleotidyltransferases

Functions and mechanisms of RNA tailing by metazoan terminal nucleotidyltransferases

TENT2, TUT4, and TUT7 selectively regulate miRNA sequence and abundance

Structure and mechanism of CutA, RNA nucleotidyl transferase with an unusual preference for cytosine

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