Evidence map›Paper›PMID 21878619›Full record

ArticleThe Journal of biological chemistry2011

Air1 zinc knuckles 4 and 5 and a conserved IWRXY motif are critical for the function and integrity of the Trf4/5-Air1/2-Mtr4 polyadenylation (TRAMP) RNA quality control complex.

Milo B Fasken, Sara W Leung, Ayan Banerjee, Maja O Kodani, Ramiro Chavez, Elizabeth A Bowman, Meghan K Purohit, Max E Rubinson, Emily H Rubinson, Anita H Corbett

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
2.7field-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

49 citing papers in PubMed, 70 citations in OpenAlex.

  1. Article
  2. TRAMP assembly alters the conformation and RNA binding of Mtr4 and Trf4-Air2.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Review
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  7. RNA Pol II Assembly Affects ncRNA Expression.International journal of molecular sciences · 2023
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  18. Article
  19. The RNA Exosome and Human Disease.Methods in molecular biology (Clifton, N.J.) · 2020
    Review
  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

10 authors at 1 institution in 1 country.

Milo B FaskenDepartment of Biochemistry, Emory University School of Medicine, Atlanta, Georgia 30322, USA. mfasken@emory.edu
Sara W Leung
Ayan Banerjee
Maja O Kodani
Ramiro Chavez
Elizabeth A Bowman
Meghan K Purohit
Max E Rubinson
Emily H Rubinson
Anita H Corbett
Emory University · US

Funding

MOLECULAR BASIS OF RAN MEDIATED NUCLEAR TRANSPORTR01GM058728 · NIGMS · EMORY UNIVERSITY · PI CORBETT, ANITA H. · 1999 to 2016
$5.4M
NIGMS NIH HHS R01 GM058728
6 · The paper itself

Abstract

In Saccharomyces cerevisiae, non-coding RNAs, including cryptic unstable transcripts (CUTs), are subject to degradation by the exosome. The Trf4/5-Air1/2-Mtr4 polyadenylation (TRAMP) complex in S. cerevisiae is a nuclear exosome cofactor that recruits the exosome to degrade RNAs. Trf4/5 are poly(A) polymerases, Mtr4 is an RNA helicase, and Air1/2 are putative RNA-binding proteins that contain five CCHC zinc knuckles (ZnKs). One central question is how the TRAMP complex, especially the Air1/2 protein, recognizes its RNA substrates. To characterize the function of the Air1/2 protein, we used random mutagenesis of the AIR1/2 gene to identify residues critical for Air protein function. We identified air1-C178R and air2-C167R alleles encoding air1/2 mutant proteins with a substitution in the second cysteine of ZnK5. Mutagenesis of the second cysteine in AIR1/2 ZnK1-5 reveals that Air1/2 ZnK4 and -5 are critical for Air protein function in vivo. In addition, we find that the level of CUT, NEL025c, in air1 ZnK1-5 mutants is stabilized, particularly in air1 ZnK4, suggesting a role for Air1 ZnK4 in the degradation of CUTs. We also find that Air1/2 ZnK4 and -5 are critical for Trf4 interaction and that the Air1-Trf4 interaction and Air1 level are critical for TRAMP complex integrity. We identify a conserved IWRXY motif in the Air1 ZnK4-5 linker that is important for Trf4 interaction. We also find that hZCCHC7, a putative human orthologue of Air1 that contains the IWRXY motif, localizes to the nucleolus in human cells and interacts with both mammalian Trf4 orthologues, PAPD5 and PAPD7 (PAP-associated domain containing 5 and 7), suggesting that hZCCHC7 is the Air component of a human TRAMP complex.

Indexed as

Adaptor Proteins, Signal TransducingAmino Acid MotifsAmino Acid SubstitutionCell NucleolusChromosomal Proteins, Non-HistoneDEAD-box RNA HelicasesDNA-Directed DNA PolymeraseDNA-Directed RNA PolymerasesHumansMultiprotein ComplexesMutagenesisMutation, MissenseRNA, FungalRNA NucleotidyltransferasesRNA StabilitySaccharomyces cerevisiaeAdaptor Proteins, Signal TransducingAir1 protein, S cerevisiaeAir2 protein, S cerevisiaeChromosomal Proteins, Non-HistoneDEAD-box RNA HelicasesDNA-Directed DNA PolymeraseDNA-Directed RNA PolymerasesMTR4 protein, S cerevisiaeMultiprotein ComplexesPAP2 protein, S cerevisiaeRNA, FungalRNA NucleotidyltransferasesSaccharomyces cerevisiae ProteinsTENT4A protein, humanTENT4B protein, humanTranscription FactorsTrf5 protein, S cerevisiaeZCCHC7 protein, human

Identifiers

PMID21878619
PMCPMC3199490
OpenAlexW2072879155

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.