Evidence map›Paper›PMID 27940556›Full record

ArticleNucleic acids research2017

The Drosophila telomere-capping protein Verrocchio binds single-stranded DNA and protects telomeres from DNA damage response.

Alessandro Cicconi, Emanuela Micheli, Fiammetta Vernì, Alison Jackson, Ana Citlali Gradilla, Francesca Cipressa, Domenico Raimondo, Giuseppe Bosso, James G Wakefield, Laura Ciapponi and 4 more

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.1field-weighted citation impact, top 12% 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

12 citing papers in PubMed, 21 citations in OpenAlex.

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  10. Studying protein-DNA interactions using atomic force microscopy.Seminars in cell & developmental biology · 2018
    Review
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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

14 authors at 3 institutions in 2 countries.

Alessandro CicconiDipartimento di Biologia e Biotecnologie 'C. Darwin', Sapienza, Università di Roma, 00185 Roma, Italy.
Emanuela MicheliDipartimento di Biologia e Biotecnologie 'C. Darwin', Sapienza, Università di Roma, 00185 Roma, Italy.
Fiammetta VernìDipartimento di Biologia e Biotecnologie 'C. Darwin', Sapienza, Università di Roma, 00185 Roma, Italy.
Alison JacksonBiosciences, College of Life and Environmental Sciences, University of Exeter, Exeter EX4 4QD, UK.
Ana Citlali GradillaBiosciences, College of Life and Environmental Sciences, University of Exeter, Exeter EX4 4QD, UK.
Francesca CipressaDipartimento di Biologia e Biotecnologie 'C. Darwin', Sapienza, Università di Roma, 00185 Roma, Italy.
Domenico RaimondoDipartimento di Medicina Molecolare, Sapienza, Università di Roma, 00185 Roma, Italy.
Giuseppe BossoDipartimento di Biologia e Biotecnologie 'C. Darwin', Sapienza, Università di Roma, 00185 Roma, Italy.
James G WakefieldBiosciences, College of Life and Environmental Sciences, University of Exeter, Exeter EX4 4QD, UK.
Laura CiapponiDipartimento di Biologia e Biotecnologie 'C. Darwin', Sapienza, Università di Roma, 00185 Roma, Italy.
Giovanni CenciDipartimento di Biologia e Biotecnologie 'C. Darwin', Sapienza, Università di Roma, 00185 Roma, Italy.
Maurizio GattiDipartimento di Biologia e Biotecnologie 'C. Darwin', Sapienza, Università di Roma, 00185 Roma, Italy.
Stefano CacchioneDipartimento di Biologia e Biotecnologie 'C. Darwin', Sapienza, Università di Roma, 00185 Roma, Italy.
Grazia Daniela RaffaDipartimento di Biologia e Biotecnologie 'C. Darwin', Sapienza, Università di Roma, 00185 Roma, Italy.
Sapienza University of Rome · ITIstituto Pasteur · ITUniversity of Exeter · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Drosophila telomeres are sequence-independent structures maintained by transposition to chromosome ends of three specialized retroelements rather than by telomerase activity. Fly telomeres are protected by the terminin complex that includes the HOAP, HipHop, Moi and Ver proteins. These are fast evolving, non-conserved proteins that localize and function exclusively at telomeres, protecting them from fusion events. We have previously suggested that terminin is the functional analogue of shelterin, the multi-protein complex that protects human telomeres. Here, we use electrophoretic mobility shift assay (EMSA) and atomic force microscopy (AFM) to show that Ver preferentially binds single-stranded DNA (ssDNA) with no sequence specificity. We also show that Moi and Ver form a complex in vivo. Although these two proteins are mutually dependent for their localization at telomeres, Moi neither binds ssDNA nor facilitates Ver binding to ssDNA. Consistent with these results, we found that Ver-depleted telomeres form RPA and γH2AX foci, like the human telomeres lacking the ssDNA-binding POT1 protein. Collectively, our findings suggest that Drosophila telomeres possess a ssDNA overhang like the other eukaryotes, and that the terminin complex is architecturally and functionally similar to shelterin.

Indexed as

DNA DamageAnimalsChromosomal Proteins, Non-HistoneDNA RepairDNA, Single-StrandedDrosophilaDrosophila ProteinsMicroscopy, Atomic ForceProtein DomainsProtein MultimerizationReplication Protein ATelomereTelomere-Binding ProteinsChromosomal Proteins, Non-HistoneDNA, Single-StrandedDrosophila Proteinsmoi protein, DrosophilaReplication Protein ARpA-70 protein, DrosophilaTelomere-Binding ProteinsVer protein, Drosophila

Identifiers

PMID27940556
PMCPMC5389638
OpenAlexW2605145140

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.