Identification and characterization of propionylation at histone H3 lysine 23 in mammalian cells

Bo Liu, Yihui Lin, Agus Darwanto, Xuehui Song, Guoliang Xu, Kangling Zhang

Research output: Contribution to journalArticle

72 Citations (Scopus)

Abstract

Propionylation has been identified recently as a new type of protein post-translational modification. Bacterial propionyl-CoA synthetase and human histone H4 are propionylated at specific lysine residues that have been known previously to be acetylated. However, other proteins subject to this modification remain to be identified, and the modifying enzymes involved need to be characterized. In this work, we report the discovery of histone H3 propionylation in mammalian cells. Propionylation at H3 lysine Lys23 was detected in the leukemia cell line U937 by mass spectrometry and Western analysis using a specific antibody. In this cell line, the propionylated form of Lys23 accounted for 7%, a level at least 6-fold higher than in other leukemia cell lines (HL-60 and THP-1) or non-leukemia cell lines (HeLa and IMR-90). The propionylation level in U937 cells decreased remarkably during monocytic differentiation, indicating that this modification is dynamically regulated. Moreover, in vitro assays demonstrated that histone acetyltransferase p300 can catalyze H3 Lys23 propionylation, whereas histone deacetylase Sir2 can remove this modification in the presence of NAD+. These results suggest that histone propionylation might be generated by the same set of enzymes as for histone acetylation and that selection of donor molecules (propionyl-CoA versus acetyl-CoA) may determine the difference of modifications. Because like acetyl-CoA, propionyl-CoA is an important intermediate in biosynthesis and energy production, histone H3 Lys23 propionylation may provide a novel epigenetic regulatory mark for cell metabolism.

Original languageEnglish
Pages (from-to)32288-32295
Number of pages8
JournalJournal of Biological Chemistry
Volume284
Issue number47
DOIs
StatePublished - Nov 20 2009
Externally publishedYes

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Histones
Lysine
Cells
Cell Line
Acetyl Coenzyme A
Leukemia
Histone Acetyltransferases
Donor Selection
Acetylation
U937 Cells
Histone Deacetylases
Biosynthesis
Enzymes
Post Translational Protein Processing
Metabolism
Epigenomics
NAD
Mass spectrometry
Assays
Mass Spectrometry

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Cite this

Identification and characterization of propionylation at histone H3 lysine 23 in mammalian cells. / Liu, Bo; Lin, Yihui; Darwanto, Agus; Song, Xuehui; Xu, Guoliang; Zhang, Kangling.

In: Journal of Biological Chemistry, Vol. 284, No. 47, 20.11.2009, p. 32288-32295.

Research output: Contribution to journalArticle

Liu, Bo ; Lin, Yihui ; Darwanto, Agus ; Song, Xuehui ; Xu, Guoliang ; Zhang, Kangling. / Identification and characterization of propionylation at histone H3 lysine 23 in mammalian cells. In: Journal of Biological Chemistry. 2009 ; Vol. 284, No. 47. pp. 32288-32295.
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