Evidence map›Paper›PMID 21788334›Full record

ArticleRNA (New York, N.Y.)2011

PAPD5, a noncanonical poly(A) polymerase with an unusual RNA-binding motif.

Christiane Rammelt, Biter Bilen, Mihaela Zavolan, Walter Keller

Abstract read
In one paragraph

Article in RNA (New York, N.Y.), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing 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

53 citing papers in PubMed.

  1. Article
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  6. Gene Therapy for Skin Aging.Current gene therapy · 2025
    Review
  7. RNA tailing machinery drives amyloidogenic phase transition.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. 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

4 authors.

Christiane RammeltInstitute of Biochemistry and Biotechnology, Martin Luther University Halle-Wittenberg, D-06099 Halle, Germany. christiane.rammelt@biochemtech.uni-halle.de
Biter Bilen
Mihaela Zavolan
Walter Keller

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

PAPD5 is one of the seven members of the family of noncanonical poly(A) polymerases in human cells. PAPD5 was shown to polyadenylate aberrant pre-ribosomal RNAs in vivo, similar to degradation-mediating polyadenylation by the noncanonical poly(A) polymerase Trf4p in yeast. PAPD5 has been reported to be also involved in the uridylation-dependent degradation of histone mRNAs. To test whether PAPD5 indeed catalyzes adenylation as well as uridylation of RNA substrates, we analyzed the in vitro properties of recombinant PAPD5 expressed in mammalian cells as well as in bacteria. Our results show that PAPD5 catalyzes the polyadenylation of different types of RNA substrates in vitro. Interestingly, PAPD5 is active without a protein cofactor, whereas its yeast homolog Trf4p is the catalytic subunit of a bipartite poly(A) polymerase in which a separate RNA-binding subunit is needed for activity. In contrast to the yeast protein, the C terminus of PAPD5 contains a stretch of basic amino acids that is involved in binding the RNA substrate.

Indexed as

Amino Acid MotifsAmino Acid SequenceCatalytic DomainEscherichia coliGenes, FungalHEK293 CellsHeLa CellsHumansMolecular Sequence DataPolyadenylationPolynucleotide AdenylyltransferaseRNA-Binding ProteinsRNA, FungalRNA, RibosomalRNA, TransferSaccharomyces cerevisiaePolynucleotide AdenylyltransferaseRNA-Binding ProteinsRNA, FungalRNA, RibosomalRNA, Transfer

Identifiers

PMID21788334
PMCPMC3162338

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.