Evidence map›Paper›PMID 25979828›Full record

ArticleThe EMBO journal2015

TUT7 controls the fate of precursor microRNAs by using three different uridylation mechanisms.

Boseon Kim, Minju Ha, Luuk Loeff, Hyeshik Chang, Dhirendra K Simanshu, Sisi Li, Mohamed Fareh, Dinshaw J Patel, Chirlmin Joo, V Narry Kim

Open access · hybridAbstract read
In one paragraph

Article in The EMBO journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 81 papers.

0numbers the graph read from it
0cells of the map it votes in
81citing papers in PubMed
6.0field-weighted citation impact, top 3% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

81 citing papers in PubMed, 108 citations in OpenAlex.

  1. Article
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  3. Review
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  5. Review
  6. The biogenesis and regulation of animal microRNAs.Nature reviews. Molecular cell biology · 2025
    Review
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21 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors at 4 institutions in 3 countries.

Boseon KimCenter for RNA Research, Institute for Basic Science, Seoul, Korea School of Biological Sciences, Seoul National University, Seoul, Korea.
Minju HaCenter for RNA Research, Institute for Basic Science, Seoul, Korea School of Biological Sciences, Seoul National University, Seoul, Korea.
Luuk LoeffKavli Institute of NanoScience, Department of BioNanoScience, Delft University of Technology, Delft, The Netherlands.
Hyeshik ChangCenter for RNA Research, Institute for Basic Science, Seoul, Korea School of Biological Sciences, Seoul National University, Seoul, Korea.
Dhirendra K SimanshuStructural Biology Program, Memorial Sloan-Kettering Cancer Center, New York, NY, USA.
Sisi LiStructural Biology Program, Memorial Sloan-Kettering Cancer Center, New York, NY, USA.
Mohamed FarehKavli Institute of NanoScience, Department of BioNanoScience, Delft University of Technology, Delft, The Netherlands.
Dinshaw J PatelStructural Biology Program, Memorial Sloan-Kettering Cancer Center, New York, NY, USA.
Chirlmin JooKavli Institute of NanoScience, Department of BioNanoScience, Delft University of Technology, Delft, The Netherlands c.joo@tudelft.nl narrykim@snu.ac.kr.
V Narry KimCenter for RNA Research, Institute for Basic Science, Seoul, Korea School of Biological Sciences, Seoul National University, Seoul, Korea c.joo@tudelft.nl narrykim@snu.ac.kr.
Delft University of Technology · NLInstitute for Basic Science · KRMemorial Sloan Kettering Cancer Center · USSeoul National University · KR

Funding

X-RAY CRYSTALLOGRAPHYP30CA008748 · NCI · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI Hongbiao Carl Lekaye · 1985 to 2026
$347.4M
NCI NIH HHS P30 CA008748
6 · The paper itself

Abstract

Terminal uridylyl transferases (TUTs) function as integral regulators of microRNA (miRNA) biogenesis. Using biochemistry, single-molecule, and deep sequencing techniques, we here investigate the mechanism by which human TUT7 (also known as ZCCHC6) recognizes and uridylates precursor miRNAs (pre-miRNAs) in the absence of Lin28. We find that the overhang of a pre-miRNA is the key structural element that is recognized by TUT7 and its paralogues, TUT4 (ZCCHC11) and TUT2 (GLD2/PAPD4). For group II pre-miRNAs, which have a 1-nt 3' overhang, TUT7 restores the canonical end structure (2-nt 3' overhang) through mono-uridylation, thereby promoting miRNA biogenesis. For pre-miRNAs where the 3' end is further recessed into the stem (as in 3' trimmed pre-miRNAs), TUT7 generates an oligo-U tail that leads to degradation. In contrast to Lin28-stimulated oligo-uridylation, which is processive, a distributive mode is employed by TUT7 for both mono- and oligo-uridylation in the absence of Lin28. The overhang length dictates the frequency (but not duration) of the TUT7-RNA interaction, thus explaining how TUT7 differentiates pre-miRNA species with different overhangs. Our study reveals dual roles and mechanisms of uridylation in repair and removal of defective pre-miRNAs.

Indexed as

RNA Processing, Post-TranscriptionalAdenine NucleotidesBase SequenceHEK293 CellsHeLa CellsHumansMicroRNAsMolecular Sequence DataNucleic Acid ConformationOligoribonucleotidesRNA NucleotidyltransferasesRNA PrecursorsRNA StabilityUracil NucleotidesUridine Monophosphate2',5'-oligoadenylateAdenine NucleotidesMicroRNAsOligoribonucleotidesoligo(U)RNA NucleotidyltransferasesRNA PrecursorsTUT7 protein, humanUracil NucleotidesUridine Monophosphateprecursor microRNAsingle‐molecule fluorescenceTUT4 (ZCCHC11)TUT7 (ZCCHC6)uridylation

Identifiers

PMID25979828
PMCPMC4516432
OpenAlexW2095868857

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.