Evidence map›Paper›PMID 42231506›Full record

ArticleGenome biology2026

Dbp7 interacts with RNA exosome component Dis3 to mediate CENP-A loading to centromeres.

Jinxin Gao, Fengying Gao, Qianhua Dong, Zhe Li, Lening Mao, Muhammad Ali, Junwei Liao, Jinpu Yang, Fei Li

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Genome biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
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

1 citing paper in PubMed.

  1. Article
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

9 authors.

Jinxin Gao *Department of Biology, New York University, 24 Waverly Place, 6th Floor, New York, NY, 10003, USA.
Fengying Gao *Department of Biology, New York University, 24 Waverly Place, 6th Floor, New York, NY, 10003, USA.
Qianhua DongDepartment of Biology, New York University, 24 Waverly Place, 6th Floor, New York, NY, 10003, USA.
Zhe LiDepartment of Biology, New York University, 24 Waverly Place, 6th Floor, New York, NY, 10003, USA.
Lening MaoDepartment of Biology, New York University, 24 Waverly Place, 6th Floor, New York, NY, 10003, USA.
Muhammad AliDepartment of Biology, New York University, 24 Waverly Place, 6th Floor, New York, NY, 10003, USA.
Junwei LiaoDepartment of Biology, New York University, 24 Waverly Place, 6th Floor, New York, NY, 10003, USA.
Jinpu YangDepartment of Biology, New York University, 24 Waverly Place, 6th Floor, New York, NY, 10003, USA.
Fei LiDepartment of Biology, New York University, 24 Waverly Place, 6th Floor, New York, NY, 10003, USA. fl43@nyu.edu.

Funding

Molecular Basis of Centromere Specification and InheritanceR35GM134920 · NIGMS · NEW YORK UNIVERSITY · PI LI, FEI · 2020 to 2025
$4.2M
NIGMS NIH HHS 2R35GM134920NIGMS NIH HHS R35 GM134920
6 · The paper itself

Abstract

backgroundCentromeres are crucial for proper chromosome segregation during cell division. Centromeres in most eukaryotes are epigenetically defined by the histone H3 variant, CENP-A. Centromeric regions are typically transcribed into non-coding RNAs that contribute to centromere functions. However, the precise role of centromeric RNAs in CENP-A loading, in particular the formation of R-loops, remains poorly understood and the mechanisms that safeguard centromeres from R-loop-associated defects are still largely unclear.

resultsUsing a visual genetic screen in fission yeast, we find that a conserved ATP-dependent RNA helicase Dbp7, an RNA binding protein that plays a role in preventing accumulation of R-loops at centromeres, is a critical regulator of CENP-A loading to centromeres. Deletion of dbp7

conclusionsTogether, this study uncovers a previously unrecognized CENP-A loading mechanism, by which Dbp7 and Dis3 act together to bind to centromeric transcripts and in turn mediate recruitment of CENP-A via the CENP-A chaperone Sim3, providing mechanistic insight into R-loop resolution at centromeres.

Indexed as

CentromereCentromere Protein ADEAD-box RNA HelicasesExosome Multienzyme Ribonuclease ComplexSchizosaccharomycesSchizosaccharomyces pombe ProteinsChromosome SegregationProtein BindingR-Loop StructuresCentromere Protein ADEAD-box RNA Helicasesdis3 protein, S pombeExosome Multienzyme Ribonuclease ComplexSchizosaccharomyces pombe ProteinsCENP-A loadingCentromeresCentromeric non-coding RNADbp7Dis3ExosomeR-loopsSchizosaccharomyces pombe

Identifiers

PMID42231506
PMCPMC13445767

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Registered trials

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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.