Evidence map›Paper›PMID 33328546›Full record

ArticleCommunications biology2020

Structurally distinct telomere-binding proteins in Ustilago maydis execute non-overlapping functions in telomere replication, recombination, and protection.

Eun Young Yu, Syed S Zahid, Swapna Ganduri, Jeanette H Sutherland, Min Hsu, William K Holloman, Neal F Lue

Open access · goldAbstract read
In one paragraph

Article in Communications biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.0field-weighted citation impact, top 24% 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

10 citing papers in PubMed, 12 citations in OpenAlex.

  1. Article
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  6. Comparative genomics ofbioRxiv : the preprint server for biology · 2024
    Article
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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

7 authors at 1 institution in 1 country.

Eun Young YuDepartment of Microbiology & Immunology, W. R. Hearst Microbiology Research Center, Weill Cornell Medicine, 1300 York Avenue, New York, NY, 10065, USA.
Syed S ZahidDepartment of Microbiology & Immunology, W. R. Hearst Microbiology Research Center, Weill Cornell Medicine, 1300 York Avenue, New York, NY, 10065, USA.
Swapna GanduriDepartment of Microbiology & Immunology, W. R. Hearst Microbiology Research Center, Weill Cornell Medicine, 1300 York Avenue, New York, NY, 10065, USA.
Jeanette H SutherlandDepartment of Microbiology & Immunology, W. R. Hearst Microbiology Research Center, Weill Cornell Medicine, 1300 York Avenue, New York, NY, 10065, USA.
Min HsuDepartment of Microbiology & Immunology, W. R. Hearst Microbiology Research Center, Weill Cornell Medicine, 1300 York Avenue, New York, NY, 10065, USA.
William K HollomanDepartment of Microbiology & Immunology, W. R. Hearst Microbiology Research Center, Weill Cornell Medicine, 1300 York Avenue, New York, NY, 10065, USA.
Neal F LueDepartment of Microbiology & Immunology, W. R. Hearst Microbiology Research Center, Weill Cornell Medicine, 1300 York Avenue, New York, NY, 10065, USA. nflue@med.cornell.edu.ORCID 0000-0001-9700-6895
Cornell University · US

Funding

Telomere terminal extension and replication: mechanisms and links to DNA repair - SupplementR01GM107287 · NIGMS · WEILL MEDICAL COLL OF CORNELL UNIV · PI LUE, NEAL F · 2014 to 2023
$2.9M
NIGMS NIH HHS GM107287NIGMS NIH HHS R01 GM107287
6 · The paper itself

Abstract

Duplex telomere binding proteins exhibit considerable structural and functional diversity in fungi. Herein we interrogate the activities and functions of two Myb-containing, duplex telomere repeat-binding factors in Ustilago maydis, a basidiomycete that is evolutionarily distant from the standard fungi. These two telomere-binding proteins, UmTay1 and UmTrf2, despite having distinct domain structures, exhibit comparable affinities and sequence specificity for the canonical telomere repeats. UmTay1 specializes in promoting telomere replication and an ALT-like pathway, most likely by modulating the helicase activity of Blm. UmTrf2, in contrast, is critical for telomere protection; transcriptional repression of Umtrf2 leads to severe growth defects and profound telomere aberrations. Comparative analysis of UmTay1 homologs in different phyla reveals broad functional diversity for this protein family and provides a case study for how DNA-binding proteins can acquire and lose functions at various chromosomal locations. Our findings also point to stimulatory effect of telomere protein on ALT in Ustilago maydis that may be conserved in other systems.

Indexed as

DNA ReplicationRecombination, GeneticBasidiomycotaBinding SitesEvolution, MolecularHumansModels, MolecularProtein ConformationProto-Oncogene Proteins c-mybRepetitive Sequences, Nucleic AcidTelomereTelomere-Binding ProteinsMYB protein, humanProto-Oncogene Proteins c-mybTelomere-Binding Proteins

Identifiers

PMID33328546
PMCPMC7744550
OpenAlexW3110918148

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.