Evidence map›Paper›PMID 19619322›Full record

ArticleBMC evolutionary biology2009

Zebrafish RNase T2 genes and the evolution of secretory ribonucleases in animals.

Melissa S Hillwig, Ludmila Rizhsky, Ying Wang, Alisa Umanskaya, Jeffrey J Essner, Gustavo C MacIntosh

Open access · goldAbstract read
In one paragraph

Article in BMC evolutionary biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

18 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Plant methods · 2020
    Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. rnaset2 mutant zebrafish model familial cystic leukoencephalopathy and reveal a role for RNase T2 in degrading ribosomal RNA.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  16. RNS2, a conserved member of the RNase T2 family, is necessary for ribosomal RNA decay in plants.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  17. Article
  18. Natural History of Innate Host Defense Peptides.Probiotics and antimicrobial proteins · 2009
    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

6 authors at 1 institution in 1 country.

Melissa S HillwigInterdepartmental Genetics Graduate Program, Iowa State University, Ames, IA 50011, USA. mfeile@iastate.edu
Ludmila Rizhsky
Ying Wang
Alisa Umanskaya
Jeffrey J Essner
Gustavo C MacIntosh
Iowa State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundMembers of the Ribonuclease (RNase) T2 family are common models for enzymological studies, and their evolution has been well characterized in plants. This family of acidic RNases is widespread, with members in almost all organisms including plants, animals, fungi, bacteria and even some viruses. While several biological functions have been proposed for these enzymes in plants, their role in animals is unknown. Interestingly, in vertebrates most of the biological roles of plant RNase T2 proteins are carried out by members of a different family, RNase A. Still, RNase T2 proteins are conserved in these animals

resultsAs a first step to shed light on the role of animal RNase T2 enzymes, and to understand the evolution of these proteins while co-existing with the RNase A family, we characterized RNase Dre1 and RNase Dre2, the two RNase T2 genes present in the zebrafish (Danio rerio) genome. These genes are expressed in most tissues examined, including high expression in all stages of embryonic development, and their expression corresponds well with the presence of acidic RNase activities in every tissue analyzed. Embryo expression seems to be a conserved characteristic of members of this family, as other plant and animal RNase T2 genes show similar high expression during embryo development. While plant RNase T2 proteins and the vertebrate RNase A family show evidences of radiation and gene sorting, vertebrate RNase T2 proteins form a monophyletic group, but there is also another monophyletic group defining a fish-specific RNase T2 clade.

conclusionBased on gene expression and phylogenetic analyses we propose that RNase T2 enzymes carry out a housekeeping function. This conserved biological role probably kept RNase T2 enzymes in animal genomes in spite of the presence of RNases A. A hypothetical role during embryo development is also discussed.

Indexed as

Evolution, MolecularAmino Acid SequenceAnimalsCloning, MolecularDNA, ComplementaryEmbryo, NonmammalianEndoribonucleasesFemaleFish ProteinsGene ExpressionGene Expression ProfilingMaleMolecular Sequence DataPhylogenySequence AlignmentSequence Analysis, DNADNA, ComplementaryEndoribonucleasesFish Proteinsribonuclease T(2)

Identifiers

PMID19619322
PMCPMC2720953
OpenAlexW2135345646

What OpenQuestion 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 OpenQuestion graph.