Evidence map›Paper›PMID 35197365›Full record

ArticleRNA (New York, N.Y.)2022

The Pet127 protein is a mitochondrial 5'-to-3' exoribonuclease from the PD-(D/E)XK superfamily involved in RNA maturation and intron degradation in yeasts.

Karolina Łabędzka-Dmoch, Michal Rażew, Marta Gapińska, Jakub Piątkowski, Adam Kolondra, Hanna Salmonowicz, Joanna M Wenda, Marcin Nowotny, Paweł Golik

Abstract read
In one paragraph

Article in RNA (New York, N.Y.), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. How RNases Shape Mitochondrial Transcriptomes.International journal of molecular sciences · 2022
    Review
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.

Karolina Łabędzka-Dmoch *Institute of Genetics and Biotechnology, Faculty of Biology, University of Warsaw, Warsaw 02-106, Poland.ORCID 0000-0002-9108-7628
Michal Rażew *Laboratory of Protein Structure, International Institute of Molecular and Cell Biology, Warsaw 02-109, Poland.ORCID 0000-0003-1306-4743
Marta GapińskaLaboratory of Protein Structure, International Institute of Molecular and Cell Biology, Warsaw 02-109, Poland.ORCID 0000-0001-5676-6660
Jakub PiątkowskiInstitute of Genetics and Biotechnology, Faculty of Biology, University of Warsaw, Warsaw 02-106, Poland.ORCID 0000-0002-7452-593X
Adam KolondraInstitute of Genetics and Biotechnology, Faculty of Biology, University of Warsaw, Warsaw 02-106, Poland.ORCID 0000-0001-5849-7185
Hanna SalmonowiczInstitute of Genetics and Biotechnology, Faculty of Biology, University of Warsaw, Warsaw 02-106, Poland.ORCID 0000-0002-9444-1039
Joanna M WendaInstitute of Genetics and Biotechnology, Faculty of Biology, University of Warsaw, Warsaw 02-106, Poland.ORCID 0000-0002-7312-6777
Marcin NowotnyLaboratory of Protein Structure, International Institute of Molecular and Cell Biology, Warsaw 02-109, Poland.ORCID 0000-0001-8632-0977
Paweł GolikInstitute of Genetics and Biotechnology, Faculty of Biology, University of Warsaw, Warsaw 02-106, Poland.ORCID 0000-0001-7814-482X

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Pet127 is a mitochondrial protein found in multiple eukaryotic lineages, but absent from several taxa, including plants and animals. Distant homology suggests that it belongs to the divergent PD-(D/E)XK superfamily which includes various nucleases and related proteins. Earlier yeast genetics experiments suggest that it plays a nonessential role in RNA degradation and 5' end processing. Our phylogenetic analysis suggests that it is a primordial eukaryotic invention that was retained in diverse groups, and independently lost several times in the evolution of other organisms. We demonstrate for the first time that the fungal Pet127 protein in vitro is a processive 5'-to-3' exoribonuclease capable of digesting various substrates in a sequence nonspecific manner. Mutations in conserved residues essential in the PD-(D/E)XK superfamily active site abolish the activity of Pet127. Deletion of the

Indexed as

ExoribonucleasesRNACandida albicansFungal ProteinsIntronsMitochondrial ProteinsPhylogenyExoribonucleasesFungal ProteinsMitochondrial ProteinsRNACandida albicansexoribonucleaseintronsmitochondriaPet127RNA degradation

Identifiers

PMID35197365
PMCPMC9014873

What Socratic 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 Socratic graph.