Evidence map›Paper›PMID 23912279›Full record

ArticleNature structural & molecular biology2013

Molecular basis for N-terminal acetylation by the heterodimeric NatA complex.

Glen Liszczak, Jacob M Goldberg, Håvard Foyn, E James Petersson, Thomas Arnesen, Ronen Marmorstein

Abstract read
In one paragraph

Article in Nature structural & molecular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 107 papers.

0numbers the graph read from it
0cells of the map it votes in
107citing 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

107 citing papers in PubMed.

  1. Trial
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Acetyltransferase in cardiovascular disease and aging.The journal of cardiovascular aging · 2024
    Article
  20. Article

47 more citing papers are in PubMed but not listed here.

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

6 authors.

Glen Liszczak1] Program in Gene Expression and Regulation, Wistar Institute, Philadelphia, Pennsylvania, USA. [2] Department of Chemistry, University of Pennsylvania, Philadelphia, Pennsylvania, USA.
Jacob M Goldberg
Håvard Foyn
E James Petersson
Thomas Arnesen
Ronen Marmorstein

Funding

Tumor Microenvironment and MetastasisP30CA010815 · NCI · WISTAR INSTITUTE · PI Luis J Montaner · 1985 to 2026
$75.9M
Structure/Function of Histone AcetyltransferasesR01GM060293 · NIGMS · WISTAR INSTITUTE · PI MARMORSTEIN, RONEN · 2000 to 2016
$5.3M
Predoctoral Training at the Chemistry-Biology InterfaceT32GM071339 · NIGMS · WISTAR INSTITUTE · PI MARMORSTEIN, RONEN, SPEICHER, DAVID W. · 2005 to 2019
$3.2M
NCI NIH HHS CA010815NCI NIH HHS P30 CA010815NIGMS NIH HHS GM060293NIGMS NIH HHS GM071339NIGMS NIH HHS R01 GM060293NIGMS NIH HHS T32 GM071339
6 · The paper itself

Abstract

N-terminal acetylation is ubiquitous among eukaryotic proteins and controls a myriad of biological processes. Of the N-terminal acetyltransferases (NATs) that facilitate this cotranslational modification, the heterodimeric NatA complex has the most diversity for substrate selection and modifies the majority of all N-terminally acetylated proteins. Here, we report the X-ray crystal structure of the 100-kDa holo-NatA complex from Schizosaccharomyces pombe, in the absence and presence of a bisubstrate peptide-CoA-conjugate inhibitor, as well as the structure of the uncomplexed Naa10p catalytic subunit. The NatA-Naa15p auxiliary subunit contains 13 tetratricopeptide motifs and adopts a ring-like topology that wraps around the NatA-Naa10p subunit, an interaction that alters the Naa10p active site for substrate-specific acetylation. These studies have implications for understanding the mechanistic details of other NAT complexes and how regulatory subunits modulate the activity of the broader family of protein acetyltransferases.

Indexed as

AcetyltransferasesAllosteric RegulationAmino Acid SequenceAnimalsCatalytic DomainCrystallography, X-RayHoloenzymesHumansKineticsModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedN-Terminal Acetyltransferase AProtein Structure, QuaternaryProtein SubunitsSchizosaccharomycesAcetyltransferasesHoloenzymesNatA protein, S pombeN-Terminal Acetyltransferase AProtein SubunitsSchizosaccharomyces pombe Proteins

Identifiers

PMID23912279
PMCPMC3766382

What OpenQuestion holds

Textmetadata
LicenceTDM
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.