Evidence map›Paper›PMID 19332560›Full record

ArticleMolecular and cellular biology2009

Properties of Nat4, an N(alpha)-acetyltransferase of Saccharomyces cerevisiae that modifies N termini of histones H2A and H4.

Bogdan Polevoda, Jason Hoskins, Fred Sherman

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

31 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
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  11. The Roles of Chromatin Accessibility in Regulating theJournal of fungi (Basel, Switzerland) · 2021
    Review
  12. Development of A Continuous Fluorescence-Based Assay forInternational journal of molecular sciences · 2021
    Article
  13. Article
  14. Article
  15. Actin's N-terminal acetyltransferase uncovered.Cytoskeleton (Hoboken, N.J.) · 2018
    Article
  16. Article
  17. Article
  18. High expression of Naa10p associates with lymph node metastasis and predicts favorable prognosis of oral squamous cell carcinoma.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2016
    Article
  19. 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

3 authors at 1 institution in 1 country.

Bogdan PolevodaDepartment of Biochemistry and Biophysics, University of Rochester Medical Center, Rochester, NY 14642, USA.
Jason Hoskins
Fred Sherman
University of Rochester Medical Center · US

Funding

Regulation and Gene Expression of Yeast Cytochrome cR01GM012702 · NIGMS · UNIVERSITY OF ROCHESTER · PI SHERMAN, FRED · 1985 to 2010
$4.3M
MALDI-TOF MASS SPECTROMETERS10RR014682 · NCRR · UNIVERSITY OF ROCHESTER · PI ANDERS, MARION W · 2000 to 2000
$265k
NCRR NIH HHS RR14682NIGMS NIH HHS GM12702NIGMS NIH HHS R01 GM012702
6 · The paper itself

Abstract

Nat4, also designated NatD, was previously shown to acetylate the N termini of histones H2A and H4, which have SGGKG and SGRGK N termini (O. K. Song, X. Wang, J. H. Waterborg, and R. Sternglanz, J. Biol. Chem. 278:38109-38112, 2003). The analysis of chimeric proteins with various N-terminal segments of histone H4 fused to iso-1-cytochrome c revealed that efficient acetylation by NatD required at least 30 to 50 amino acid residues of the N terminus of histone H4. This requirement for an extended N terminus is in marked contrast with the major N-terminal acetyl transferases (NATs), i.e., NatA, NatB, and NatC, which require as few as two specific residues and usually no more than four or five. However, similar to the other NATs, NatD is associated with ribosomes. The nat4-Delta strain showed several minor phenotypes, including sensitivity to 3-aminotriazole, benomyl, and thiabendazole. Moreover, these nat4-Delta phenotypes were enhanced in the strain containing K5R K8R K12R replacements in the N-tail of histone H4, suggesting that the lack of N-terminal serine acetylation is synergistic to the lack of acetylation of the H4 N-tail lysines. Thus, N-terminal serine acetylation of histone H4 may be a part of an essential charge patch first described for the histone H2A.Z variant in Tetrahymena species.

Indexed as

Protein Processing, Post-TranslationalAcetylationAcetyltransferasesAllelesAmino Acid SequenceCentrifugation, Density GradientCytochromes cHistone AcetyltransferasesHistonesMolecular Sequence DataMutationN-Terminal Acetyltransferase DPhenotypePolyribosomesProtein Structure, SecondaryProtein TransportAcetyltransferasesCYC1 protein, S cerevisiaeCytochromes cHistone AcetyltransferasesHistonesNAT4 protein, S cerevisiaeN-Terminal Acetyltransferase DRecombinant Fusion ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID19332560
PMCPMC2682015
OpenAlexW2095135425

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.