Evidence map›Paper›PMID 9199348›Full record

ArticleMolecular and cellular biology1997

The rRNA-processing function of the yeast U14 small nucleolar RNA can be rescued by a conserved RNA helicase-like protein.

W Q Liang, J A Clark, M J Fournier

Abstract read
In one paragraph

Article in Molecular and cellular biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing 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

42 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Powering through ribosome assembly.RNA (New York, N.Y.) · 2009
    Review
  14. Identification of protein binding sites on U3 snoRNA and pre-rRNA by UV cross-linking and high-throughput analysis of cDNAs.Proceedings of the National Academy of Sciences of the United States of America · 2009
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Role of RNA helicases in HIV-1 replication.Nucleic acids research · 2006
    Review
  20. 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

3 authors.

W Q LiangDepartment of Biochemistry and Molecular Biology, University of Massachusetts, Amherst 01003, USA.
J A Clark
M J Fournier

Funding

BIOSYNTHESIS OF TRANSFER, 4.5S &6S RIBONUCLEIC ACIDSR01GM019351 · NIGMS · UNIVERSITY OF MASSACHUSETTS AMHERST · PI FOURNIER, MAURILLE J · 1985 to 2008
$3.3M
NIGMS NIH HHS GM19351
6 · The paper itself

Abstract

The phylogenetically conserved U14 small nucleolar RNA is required for processing of rRNA, and this function involves base pairing with conserved complementary sequences in 18S RNA. With a view to identifying other important U14 interactions, a stem-loop domain required for activity of Saccharomyces cerevisiae U14 RNAs (the Y domain) was first subjected to detailed mutational analysis. The mapping results showed that most nucleotides of the Y domain can be replaced without affecting function, except for loop nucleotides conserved among five different yeast species. Defective variants were then used to identify both intragenic and extragenic suppressor mutations. All of the intragenic mutations mapped within six nucleotides of the primary mutation, suggesting that suppression involves a change in conformation and that the loop element is involved in an essential intermolecular interaction rather than intramolecular base pairing. A high-copy extragenic suppressor gene, designated DBP4 (DEAD box protein 4), encodes an essential, putative RNA helicase of the DEAD-DEXH box family. Suppression by DBP4 (initially CA4 [T.-H. Chang, J. Arenas, and J. Abelson, Proc. Natl. Acad. Sci. USA 87:1571-1575, 1990]) restores the level of 18S rRNA and is specific for the Y domain but is not allele specific. DBP4 is predicted to function either in assembly of the U14 small nucleolar RNP or, more likely, in its interaction with other components of the rRNA processing apparatus. Mediating the interaction of U14 with precursor 18S RNA is an especially attractive possibility.

Indexed as

RNA Processing, Post-TranscriptionalSaccharomyces cerevisiae ProteinsAmino Acid SequenceBase SequenceCell NucleolusDEAD-box RNA HelicasesHydrogen BondingMolecular Sequence DataNucleic Acid ConformationRNA, FungalRNA HelicasesRNA NucleotidyltransferasesRNA, RibosomalRNA, Small NuclearSaccharomyces cerevisiaeDEAD-box RNA HelicasesHCA4 protein, S cerevisiaeRNA, FungalRNA HelicasesRNA NucleotidyltransferasesRNA, RibosomalRNA, Small NuclearSaccharomyces cerevisiae Proteins

Identifiers

PMID9199348
PMCPMC232266

What OpenQuestion holds

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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.