Identification and Characterization of Propionylation at Histone H3 Lysine 23 in Mammalian Cells

	Identification and Characterization of Propionylation at Histone H3 Lysine 23 in Mammalian Cells
	Liu, B; Lin, YH; Darwanto, A; Song, XH; Xu, GL; Zhang, KL
刊名	JOURNAL OF BIOLOGICAL CHEMISTRY
	2009
卷号	284 期号:47 页码:32288-32295
通讯作者	Xu, GL (reprint author), Chinese Acad Sci, Shanghai Inst Biol Sci, Inst Biochem & Cell Biol, State Key Lab Mol Biol, 320 Yueyang Rd, Shanghai 200031, Peoples R China.,glxu@sibs.ac.cn ; kzhang@llu.edu
英文摘要	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 Lys(23) 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 Lys(23) 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 Lys(23) 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 acetylCoA) may determine the difference of modifications. Because like acetyl-CoA, propionyl-CoA is an important intermediate in biosynthesis and energy production, histone H3 Lys(23) propionylation may provide a novel epigenetic regulatory mark for cell metabolism.
学科主题	Biochemistry & Molecular Biology
类目[WOS]	Biochemistry & Molecular Biology
关键词[WOS]	METHYLATION ; LINE ; BUTYRYLATION ; ACETYLATION ; HDOT1L ; U937 ; GENE
收录类别	SCI
语种	英语
WOS记录号	WOS:000272028400010
内容类型	期刊论文
版本	出版稿
源URL	[http://202.127.25.143/handle/331003/1300]
专题	上海生化细胞研究所_上海生科院生化细胞研究所
推荐引用方式 GB/T 7714	Liu, B,Lin, YH,Darwanto, A,et al. Identification and Characterization of Propionylation at Histone H3 Lysine 23 in Mammalian Cells[J]. JOURNAL OF BIOLOGICAL CHEMISTRY,2009,284(47):32288-32295.
APA	Liu, B,Lin, YH,Darwanto, A,Song, XH,Xu, GL,&Zhang, KL.(2009).Identification and Characterization of Propionylation at Histone H3 Lysine 23 in Mammalian Cells.JOURNAL OF BIOLOGICAL CHEMISTRY,284(47),32288-32295.
MLA	Liu, B,et al."Identification and Characterization of Propionylation at Histone H3 Lysine 23 in Mammalian Cells".JOURNAL OF BIOLOGICAL CHEMISTRY 284.47(2009):32288-32295.