Evidence map›Paper›PMID 29311576›Full record

ArticleNature communications2018

Structural analysis of mtEXO mitochondrial RNA degradosome reveals tight coupling of nuclease and helicase components.

Michal Razew, Zbigniew Warkocki, Michal Taube, Adam Kolondra, Mariusz Czarnocki-Cieciura, Elzbieta Nowak, Karolina Labedzka-Dmoch, Aleksandra Kawinska, Jakub Piatkowski, Pawel Golik and 3 more

Abstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed.

  1. Article
  2. Article
  3. Mechanisms and regulation of human mitochondrial transcription.Nature reviews. Molecular cell biology · 2024
    Review
  4. Review
  5. SUV3 Helicase and Mitochondrial Homeostasis.International journal of molecular sciences · 2023
    Review
  6. How RNases Shape Mitochondrial Transcriptomes.International journal of molecular sciences · 2022
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. The pentatricopeptide repeat protein Rmd9 recognizes the dodecameric element in the 3'-UTRs of yeast mitochondrial mRNAs.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  14. Article
  15. Terminal nucleotidyl transferases (TENTs) in mammalian RNA metabolism.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018
    Review
  16. Article
  17. 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

13 authors.

Michal RazewLaboratory of Protein Structure, International Institute of Molecular and Cell Biology, Trojdena 4, 02-109, Warsaw, Poland.
Zbigniew WarkockiLaboratory of RNA Biology and Functional Genomics, Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Pawinskiego 5a, 02-106, Warsaw, Poland.
Michal TaubeFaculty of Physics, Adam Mickiewicz University, ul. Umultowska 89, 61-614, Poznan, Poland.
Adam KolondraInstitute of Genetics and Biotechnology, Faculty of Biology, University of Warsaw, Pawinskiego 5a, 02-106, Warsaw, Poland.
Mariusz Czarnocki-CieciuraLaboratory of Protein Structure, International Institute of Molecular and Cell Biology, Trojdena 4, 02-109, Warsaw, Poland.
Elzbieta NowakLaboratory of Protein Structure, International Institute of Molecular and Cell Biology, Trojdena 4, 02-109, Warsaw, Poland.
Karolina Labedzka-DmochInstitute of Genetics and Biotechnology, Faculty of Biology, University of Warsaw, Pawinskiego 5a, 02-106, Warsaw, Poland.
Aleksandra KawinskaInstitute of Genetics and Biotechnology, Faculty of Biology, University of Warsaw, Pawinskiego 5a, 02-106, Warsaw, Poland.
Jakub PiatkowskiInstitute of Genetics and Biotechnology, Faculty of Biology, University of Warsaw, Pawinskiego 5a, 02-106, Warsaw, Poland.
Pawel GolikLaboratory of RNA Biology and Functional Genomics, Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Pawinskiego 5a, 02-106, Warsaw, Poland.
Maciej KozakFaculty of Physics, Adam Mickiewicz University, ul. Umultowska 89, 61-614, Poznan, Poland.
Andrzej DziembowskiLaboratory of RNA Biology and Functional Genomics, Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Pawinskiego 5a, 02-106, Warsaw, Poland.ORCID http://orcid.org/0000-0001-8492-7572
Marcin NowotnyLaboratory of Protein Structure, International Institute of Molecular and Cell Biology, Trojdena 4, 02-109, Warsaw, Poland. mnowotny@iimcb.gov.pl.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nuclease and helicase activities play pivotal roles in various aspects of RNA processing and degradation. These two activities are often present in multi-subunit complexes from nucleic acid metabolism. In the mitochondrial exoribonuclease complex (mtEXO) both enzymatic activities are tightly coupled making it an excellent minimal system to study helicase-exoribonuclease coordination. mtEXO is composed of Dss1 3'-to-5' exoribonuclease and Suv3 helicase. It is the master regulator of mitochondrial gene expression in yeast. Here, we present the structure of mtEXO and a description of its mechanism of action. The crystal structure of Dss1 reveals domains that are responsible for interactions with Suv3. Importantly, these interactions are compatible with the conformational changes of Suv3 domains during the helicase cycle. We demonstrate that mtEXO is an intimate complex which forms an RNA-binding channel spanning its entire structure, with Suv3 helicase feeding the 3' end of the RNA toward the active site of Dss1.

Indexed as

Amino Acid SequenceBase SequenceCandida glabrataCrystallography, X-RayDEAD-box RNA HelicasesEndoribonucleasesExoribonucleasesMitochondrial ProteinsMultienzyme ComplexesNucleic Acid ConformationPolyribonucleotide NucleotidyltransferaseProtein BindingProtein ConformationRNARNA HelicasesRNA, MitochondrialDEAD-box RNA HelicasesdegradosomeDSS1 protein, S cerevisiaeEndoribonucleasesExoribonucleasesMitochondrial ProteinsMultienzyme ComplexesPolyribonucleotide NucleotidyltransferaseRNARNA HelicasesRNA, MitochondrialSaccharomyces cerevisiae ProteinsSUV3 protein, S cerevisiae

Identifiers

PMID29311576
PMCPMC5758563

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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.