Gcn5 and Esa1 function as histone crotonyltransferases to regulate crotonylation-dependent transcription.
Amino Acid Sequence
Crotonates
/ chemistry
Histone Acetyltransferases
/ genetics
Histones
/ chemistry
Lysine
/ chemistry
Mass Spectrometry
Peptides
/ analysis
Promoter Regions, Genetic
Protein Processing, Post-Translational
Saccharomyces cerevisiae
/ metabolism
Saccharomyces cerevisiae Proteins
/ genetics
Transcription Factors
/ genetics
Transcription, Genetic
Esa1-Yng2-Epl1 (Piccolo NuA4) complex
Gcn5-Ada (ADA) complex
chromatin modification
crotonylation
epigenetics
gene transcription
histone modification
post-translational modification (PTM)
Journal
The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R
Informations de publication
Date de publication:
27 12 2019
27 12 2019
Historique:
received:
23
07
2019
revised:
10
10
2019
pubmed:
9
11
2019
medline:
23
6
2020
entrez:
9
11
2019
Statut:
ppublish
Résumé
Histone post-translational modifications (PTMs) are critical for processes such as transcription. The more notable among these are the nonacetyl histone lysine acylation modifications such as crotonylation, butyrylation, and succinylation. However, the biological relevance of these PTMs is not fully understood because their regulation is largely unknown. Here, we set out to investigate whether the main histone acetyltransferases in budding yeast, Gcn5 and Esa1, possess crotonyltransferase activity.
Identifiants
pubmed: 31699900
pii: S0021-9258(20)30030-2
doi: 10.1074/jbc.RA119.010302
pmc: PMC6937567
doi:
Substances chimiques
Crotonates
0
Histones
0
Peptides
0
SPT7 protein, S cerevisiae
0
Saccharomyces cerevisiae Proteins
0
Transcription Factors
0
Epl1 protein, S cerevisiae
EC 2.3.1.48
Esa1 protein, S cerevisiae
EC 2.3.1.48
GCN5 protein, S cerevisiae
EC 2.3.1.48
Histone Acetyltransferases
EC 2.3.1.48
Lysine
K3Z4F929H6
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
20122-20134Informations de copyright
© 2019 Kollenstart et al.
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