Evidence map›Paper›PMID 7510387›Full record

ArticleNucleic acids research1994

The existence of eukaryotic ribonucleoprotein consensus sequence-type RNA-binding proteins in a prokaryote, Synechococcus 6301.

M Sugita, M Sugiura

Open access · greenAbstract readComparative Study
In one paragraph

Article in Nucleic acids research, 1994. 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
2.5field-weighted citation impact, top 10% 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, 58 citations in OpenAlex.

  1. The RRM domain-containing protein Rbp3 interacts with ribosomes and the 3' ends of mRNAs encoding photosynthesis proteins.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
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  3. Roles for theJournal of biological rhythms · 2023
    Article
  4. Article
  5. Identification of genes expressed by Cryptococcus gattii during iron deprivation.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2014
    Article
  6. Article
  7. Article
  8. Chloroplast RNA-binding proteins.Current genetics · 2003
    Review
  9. Article
  10. A family of RRM-type RNA-binding proteins specific to plant mitochondria.Proceedings of the National Academy of Sciences of the United States of America · 2002
    Article
  11. Article
  12. Article
  13. Review
  14. Article
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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

2 authors at 1 institution in 1 country.

M SugitaCenter for Gene Research, Nagoya University, Japan.
M Sugiura
Nagoya University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A group of proteins containing a conserved ribonucleoprotein consensus sequence (RNP-CS)-type RNA-binding domain (CS-RBD) of approximately 80 amino acids is present in eukaryotic cells and binds specifically to a wide variety of RNA molecules. We have isolated 12 kDa single-stranded DNA binding proteins from the unicellular cyanobacterium Synechococcus 6301. The amino-terminal sequence was determined and two distinct genomic clones were isolated from a Synechococcus 6301 genomic library. Sequence analysis revealed that two closely related proteins contain a single CS-RBD of 82 amino acids and are named as 12RNP1 and 12RNP2. Both of the CS-RBDs share the highest amino acid identity with those of chloroplast ribonucleoproteins (40-51%). The 12RNP proteins were expressed in Escherichia coli bearing plasmids encoding glutathione S-transferase/12RNP fusion proteins and subjected to in vitro nucleic acid-binding assay. Both 12RNP1 and 12RNP2 bind to RNA homopolymers poly(U) and poly(G), indicating that they might be RNA-binding proteins. This is the first example of such proteins in prokaryotes. The 12RNP1 and 12RNP2 genes are transcribed as monocistronic mRNAs and the steady-state mRNA level of 12RNP1 is over 20-fold than that of 12RNP2. Due to the easiness of genetic manipulations the cyanobacterium will provide an excellent system to analyze the function of not only cyanobacterial but also plant RNA-binding proteins.

Indexed as

Base SequenceCloning, MolecularConsensus SequenceCyanobacteriaDNA-Binding ProteinsDNA, Single-StrandedEukaryotic CellsGene ExpressionGenesMolecular Sequence DataPhylogenyProkaryotic CellsRecombinant ProteinsRibonucleotidesRNARNA-Binding ProteinsDNA-Binding ProteinsDNA, Single-StrandedRecombinant ProteinsRibonucleotidesRNARNA-Binding ProteinsRNA, Messenger

Identifiers

PMID7510387
PMCPMC307741
OpenAlexW2129337654

What OpenQuestion holds

Textmetadata
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.