Evidence map›Paper›PMID 34302485›Full record

ArticleNucleic acids research2022

Yeast Ssd1 is a non-enzymatic member of the RNase II family with an alternative RNA recognition site.

Rosemary A Bayne, Uma Jayachandran, Aleksandra Kasprowicz, Stefan Bresson, David Tollervey, Edward W J Wallace, Atlanta G Cook

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.1field-weighted citation impact, top 12% 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

20 citing papers in PubMed, 32 citations in OpenAlex.

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  14. The mRNA stability factor Khd4 defines a specific mRNA regulon for membrane trafficking in the pathogenProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  15. Article
  16. Article
  17. Post-transcriptional control of fungal cell wall synthesis.Cell surface (Amsterdam, Netherlands) · 2022
    Article
  18. Microtubule integrity regulates budding yeast RAM pathway gene expression.Frontiers in cell and developmental biology · 2022
    Article
  19. Article
  20. Article
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 2 institutions in 1 country.

Rosemary A BayneInstitute of Cell Biology and SynthSys, School of Biological Sciences, University of Edinburgh, Edinburgh EH9 3BF, UK.
Uma JayachandranWellcome Centre for Cell Biology, School of Biological Sciences, University of Edinburgh, Edinburgh EH9 3BF, UK.
Aleksandra KasprowiczWellcome Centre for Cell Biology, School of Biological Sciences, University of Edinburgh, Edinburgh EH9 3BF, UK.
Stefan BressonWellcome Centre for Cell Biology, School of Biological Sciences, University of Edinburgh, Edinburgh EH9 3BF, UK.
David TollerveyWellcome Centre for Cell Biology, School of Biological Sciences, University of Edinburgh, Edinburgh EH9 3BF, UK.
Edward W J WallaceInstitute of Cell Biology and SynthSys, School of Biological Sciences, University of Edinburgh, Edinburgh EH9 3BF, UK.ORCID 0000-0001-8025-6361
Atlanta G CookWellcome Centre for Cell Biology, School of Biological Sciences, University of Edinburgh, Edinburgh EH9 3BF, UK.ORCID 0000-0003-2087-9772
Wellcome Centre for Cell Biology · GBUniversity of Edinburgh · GB

Funding

Wellcome Trust 109916Wellcome Trust 109916/Z/15/ZWellcome Trust 200898Wellcome Trust 200898/Z/16/ZWellcome Trust 203149Wellcome Trust 208779Wellcome Trust 208779/Z/17/Z
6 · The paper itself

Abstract

Ssd1, a conserved fungal RNA-binding protein, is important in stress responses, cell division and virulence. Ssd1 is closely related to Dis3L2 of the RNase II family of nucleases, but lacks catalytic activity and likely suppresses translation of bound mRNAs. Previous studies identified RNA motifs enriched in Ssd1-associated transcripts, yet the sequence requirements for Ssd1 binding are not defined. Here, we identify precise binding sites of Ssd1 on RNA using in vivo cross-linking and cDNA analysis. These sites are enriched in 5' untranslated regions of a subset of mRNAs encoding cell wall proteins. We identified a conserved bipartite motif that binds Ssd1 with high affinity in vitro. Active RNase II enzymes have a characteristic, internal RNA binding path; the Ssd1 crystal structure at 1.9 Å resolution shows that remnants of regulatory sequences block this path. Instead, RNA binding activity has relocated to a conserved patch on the surface of the protein. Structure-guided mutations of this surface prevent Ssd1 from binding RNA in vitro and phenocopy Ssd1 deletion in vivo. These studies provide a new framework for understanding the function of a pleiotropic post-transcriptional regulator of gene expression and give insights into the evolution of regulatory and binding elements in the RNase II family.

Indexed as

ExoribonucleasesSaccharomyces cerevisiaeSaccharomyces cerevisiae Proteins5' Untranslated RegionsRNA, Messenger5' Untranslated Regionsexoribonuclease IIExoribonucleasesRNA, MessengerSaccharomyces cerevisiae ProteinsSsd1 protein, S cerevisiae

Identifiers

PMID34302485
PMCPMC8934651
OpenAlexW3184128910

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

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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.