Forskning ved Københavns Universitet - Københavns Universitet


Gcn5 and Esa1 function as histone crotonyltransferases to regulate crotonylation-dependent transcription

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

  • Leonie Kollenstart
  • Anton J L de Groot
  • George M C Janssen
  • Xue Cheng
  • Kees Vreeken
  • Fabrizio Martino
  • Jacques Côté
  • Peter A van Veelen
  • Haico van Attikum

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. In vitro studies revealed that the Gcn5-Ada2-Ada3 (ADA) and Esa1-Yng2-Epl1 (Piccolo NuA4) histone acetyltransferase complexes have the capacity to crotonylate histones. Mass spectrometry analysis revealed that ADA and Piccolo NuA4 crotonylate lysines in the N-terminal tails of histone H3 and H4, respectively. Functionally, we show that crotonylation selectively affects gene transcription in vivo in a manner dependent on Gcn5 and Esa1. Thus, we identify the Gcn5- and Esa1-containing ADA and Piccolo NuA4 complexes as bona fide crotonyltransferases that promote crotonylation-dependent transcription.

TidsskriftThe Journal of Biological Chemistry
Udgave nummer52
Sider (fra-til)20122-20134
Antal sider13
StatusUdgivet - 27 dec. 2019
Eksternt udgivetJa

ID: 242624112