Evidence map›Paper›PMID 34403479›Full record

ArticleNucleic acids research2021

Arabidopsis retains vertebrate-type telomerase accessory proteins via a plant-specific assembly.

Jiarui Song, Claudia Castillo-González, Zeyang Ma, Dorothy E Shippen

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2021. 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
0.8field-weighted citation impact, top 28% 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, 13 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

4 authors at 2 institutions in 2 countries.

Jiarui SongDepartment of Biochemistry and Biophysics, Texas A&M University, College Station, TX 77843-2128, USA.
Claudia Castillo-GonzálezDepartment of Biochemistry and Biophysics, Texas A&M University, College Station, TX 77843-2128, USA.
Zeyang MaNational Maize Improvement Center of China, China Agricultural University, 100193 Beijing, China.
Dorothy E ShippenDepartment of Biochemistry and Biophysics, Texas A&M University, College Station, TX 77843-2128, USA.ORCID 0000-0003-0562-2047
Texas A&M University · USChina Agricultural University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The recent discovery of the bona-fide telomerase RNA (TR) from plants reveals conserved and unique secondary structure elements and the opportunity for new insight into the telomerase RNP. Here we examine how two highly conserved proteins previously implicated in Arabidopsis telomere maintenance, AtPOT1a and AtNAP57 (dyskerin), engage plant telomerase. We report that AtPOT1a associates with Arabidopsis telomerase via interaction with TERT. While loss of AtPOT1a does not impact AtTR stability, the templating domain is more accessible in pot1a mutants, supporting the conclusion that AtPOT1a stimulates telomerase activity but does not facilitate telomerase RNP assembly. We also show, that despite the absence of a canonical H/ACA binding motif within AtTR, dyskerin binds AtTR with high affinity and specificity in vitro via a plant specific three-way junction (TWJ). A core element of the TWJ is the P1a stem, which unites the 5' and 3' ends of AtTR. P1a is required for dyskerin-mediated stimulation of telomerase repeat addition processivity in vitro, and for AtTR accumulation and telomerase activity in vivo. The deployment of vertebrate-like accessory proteins and unique RNA structural elements by Arabidopsis telomerase provides a new platform for exploring telomerase biogenesis and evolution.

Indexed as

AnimalsArabidopsisArabidopsis ProteinsNuclear ProteinsPhylogenyProtein Structure, SecondaryRNARNA-Binding ProteinsTelomeraseTelomereTelomere-Binding ProteinsArabidopsis ProteinsNAP57 protein, ArabidopsisNuclear ProteinsPOT1A protein, ArabidopsisRNARNA-Binding ProteinsTelomerasetelomerase RNATelomere-Binding Proteins

Identifiers

PMID34403479
PMCPMC8450087
OpenAlexW3193728430

What OpenQuestion holds

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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.