Evidence map›Paper›PMID 20923774›Full record

ArticleThe Journal of biological chemistry2010

Tay1 protein, a novel telomere binding factor from Yarrowia lipolytica.

Juraj Kramara, Smaranda Willcox, Stanislava Gunisova, Slavomir Kinsky, Jozef Nosek, Jack D Griffith, Lubomir Tomaska

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
0.3field-weighted citation impact, top 42% 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

19 citing papers in PubMed, 34 citations in OpenAlex.

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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 3 institutions in 2 countries.

Juraj KramaraDepartment of Genetics, Comenius University, Faculty of Natural Sciences, Mlynska dolina, 842 15 Bratislava, Slovakia.
Smaranda Willcox
Stanislava Gunisova
Slavomir Kinsky
Jozef Nosek
Jack D Griffith
Lubomir Tomaska
Comenius University Bratislava · SKUNC Lineberger Comprehensive Cancer CenterUniversity of North Carolina at Chapel Hill · US

Funding

HOMOLOOUS RECOMBINATION: ITS MOLECULAR CYTOLOGYR01GM031819 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI GRIFFITH, JACK D · 1985 to 2017
$5.2M
Nucleoprotein structures formed at sites of DNA damageR01ES013773 · NIEHS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI GRIFFITH, JACK D · 2005 to 2015
$3.2M
Studies of Telomere Structure Using Yeast Model SystemsR03TW005654 · FIC · UNIV OF NORTH CAROLINA CHAPEL HILL · PI GRIFFITH, JACK D · 2001 to 2008
$227k
The structure of the telomere as a sentinel of DNA damage.R56ES013773 · NIEHS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI GRIFFITH, JACK D · 2019 to 2019
$150k
FIC NIH HHS R03 TW005654FIC NIH HHS TW005654Howard Hughes Medical Institute 55005622NIEHS NIH HHS ES013773NIEHS NIH HHS R01 ES013773NIEHS NIH HHS R56 ES013773NIGMS NIH HHS GM31819NIGMS NIH HHS R01 GM031819
6 · The paper itself

Abstract

Inspection of the complete genome of the yeast Yarrowia lipolytica for the presence of genes encoding homologues of known telomere-binding proteins surprisingly revealed no counterparts of typical yeast Myb domain-containing telomeric factors including Rap1 or Taz1. Instead, we identified a gene, YALIOD10923g, encoding a protein containing two Myb domains, exhibiting a high degree of similarity to the Myb domain of human telomeric proteins TRF1 and TRF2 and homologous to an essential fission yeast protein Mug152 whose expression is elevated during meiosis. The protein, which we named Tay1p (telomere-associated in Yarrowia lipolytica 1), was purified for biochemical studies. Using a model Y. lipolytica telomere, we demonstrate that the protein preferentially binds to Y. lipolytica telomeric tracts. Tay1p binds along the telomeric tract as dimers and larger oligomers, and it is able to remodel the telomeric DNA into both looped structures and synaptic complexes of two model telomere DNAs. The ability of Tay1p to induce dimerization of telomeres in vitro goes in line with its oligomeric nature, where each oligomer can employ several Myb domains to form intermolecular telomere clusters. We also provide experimental evidence that Tay1p may be associated with Y. lipolytica telomeres in vivo. Together with its homologues from Schizosaccharomyces pombe and several basidiomycetous fungi (Sánchez-Alonso, P., and Guzman, P. (2008) Fungal Genet. Biol. 45, S54-S62), Tay1p constitutes a novel family of putative telomeric factors whose analysis may be instrumental in understanding the function and evolution of double-stranded DNA telomeric proteins.

Indexed as

BasidiomycotaDimerizationDNA, FungalFungal ProteinsHumansSchizosaccharomycesSequence Homology, Amino AcidTelomereTelomere-Binding ProteinsYarrowiaDNA, FungalFungal ProteinsTelomere-Binding Proteins

Identifiers

PMID20923774
PMCPMC2992242
OpenAlexW2015635728

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.