Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

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

Molecular and cellular biology - 1 Jun 2009

Polevoda Bogdan, Hoskins Jason, Sherman Fred

Abstract excerpt

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...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Acetylation
Share to Acetyltransferases
Share to Centrifugation, Density Gradient

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Cytochromes c

Share to Histone Acetyltransferases

Share to Histones

Share to Polyribosomes

Share to Protein Processing, Post-Translational

Source

Open in PubMed Open full text

Identifiers

PMID: 19332560
DOI: 10.1128/MCB.00147-08
PMCID: PMC2682015

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Properties of Nat4, an N(alpha)-acetyltransferase of Saccharomyces cerevisiae that modifies N termini of histones H2A and H4.PMID 19332560Read ↗

NAT2, an essential gene encoding methionine N alpha-acetyltransferase in the yeast Saccharomyces cerevisiae.Semantic proximity Read ↗

An Nalpha-acetyltransferase responsible for acetylation of the N-terminal residues of histones H4 and H2A.Semantic proximity Read ↗

NatC Nalpha-terminal acetyltransferase of yeast contains three subunits, Mak3p, Mak10p, and Mak31p.Semantic proximity Read ↗

A Saccharomyces cerevisiae model reveals in vivo functional impairment of the Ogden syndrome N-terminal acetyltransferase NAA10 Ser37Pro mutant.Semantic proximity Read ↗

Cellular effects of NAT-mediated histone N-terminal acetylationSemantic proximity Read ↗

[Cloning and analysis of a novel gene encoding N-terminal acetyltransferase subunit].Semantic proximity Read ↗

Proteomics analyses reveal the evolutionary conservation and divergence of N-terminal acetyltransferases from yeast and humansSemantic proximity Read ↗

NatF Contributes to an Evolutionary Shift in Protein N-Terminal Acetylation and Is Important for Normal Chromosome SegregationSemantic proximity Read ↗

Nα-terminal Acetylation of Eukaryotic ProteinsSemantic proximity Read ↗

The nonessential H2A N-terminal tail can function as an essential charge patch on the H2A.Z variant N-terminal tail.Semantic proximity Read ↗

Dependence of ORC silencing function on NatA-mediated Nalpha acetylation in Saccharomyces cerevisiae.Semantic proximity Read ↗

Regulators of cellular levels of histone acetylation in Saccharomyces cerevisiae.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.