SIRT1 regulates the histone methyl-transferase SUV39H1 during heterochromatin formation

被引：0

作者：

Alejandro Vaquero

Michael Scher

Hediye Erdjument-Bromage

Paul Tempst

Lourdes Serrano

Danny Reinberg

机构：

[1] Howard Hughes Medical Institute,Division of Nucleic Acids Enzymology, Department of Biochemistry

[2] University of Medicine and Dentistry of New Jersey,Department of Genetics

[3] Robert Wood Johnson Medical School,Department of Biochemistry

[4] Human Genetics Institute,undefined

[5] Rutgers University,undefined

[6] 145 Bevier Road,undefined

[7] Piscataway,undefined

[8] New Jersey 08854,undefined

[9] USA,undefined

[10] NYU-Medical School,undefined

[11] 522 First Avenue,undefined

[12] New York,undefined

[13] New York 10016,undefined

[14] USA,undefined

[15] Molecular Biology Program,undefined

[16] Memorial Sloan Kettering Cancer Center,undefined

[17] 1275 York Avenue,undefined

[18] New York,undefined

[19] New York 10021,undefined

[20] USA ,undefined

[21] Present address: ICREA and IBMB-CSIC/IRB,undefined

[22] Parc Cientific de Barcelona,undefined

[23] Josep Samitier 1–5,undefined

[24] 08028 Barcelona,undefined

[25] Spain.,undefined

来源：

Nature | 2007年 / 450卷

关键词：

D O I：

暂无

中图分类号：

学科分类号：

摘要：

SUV39H1 is the major methyltransferase responsible for tri-methylation of histone H3 at lysine 9 in heterochromatin. The histone deacetylase SIRT1 is shown to target the SUV39H1 enzyme and contribute to elevated levels of SUV39H1 activity and H3K9me3 in heterochromatin.

引用

页码：440 / 444

页数：4

共 50 条

[31] The methyltransferase Suv39h1 links the SUMO pathway to HP1α marking at pericentric heterochromatin
Christèle Maison
Delphine Bailly
Jean-Pierre Quivy
Geneviève Almouzni
Nature Communications, 7
[32] Epigenetic regulation of telomere length in mammalian cells by the Suv39h1 and Suv39h2 histone methyltransferases
García-Cao, M
O'Sullivan, R
Peters, AHFM
Jenuwein, T
Blasco, MA
NATURE GENETICS, 2004, 36 (01) : 94 - 99
[33] The methyltransferase Suv39h1 links the SUMO pathway to HP1α marking at pericentric heterochromatin
Maison, Christele
Bailly, Delphine
Quivy, Jean-Pierre
Almouzni, Genevieve
NATURE COMMUNICATIONS, 2016, 7
[34] RETRACTED: Pericentric Heterochromatin Generated by HP1 Protein Interaction-defective Histone Methyltransferase Suv39h1 (Retracted Article)
Muramatsu, Daisuke
Singh, Prim B.
Kimura, Hiroshi
Tachibana, Makoto
Shinkai, Yoichi
JOURNAL OF BIOLOGICAL CHEMISTRY, 2013, 288 (35) : 25285 - 25296
[35] A two-state activation mechanism controls the histone methyltransferase Suv39h1
Müller M.M.
Fierz B.
Bittova L.
Liszczak G.
Muir T.W.
Nature Chemical Biology, 2016, 12 (3) : 188 - 193
[36] Histone Methyltransferase SUV39H2 Supports Nasopharyngeal Carcinoma Cell Metastasis by Regulation of SIRT1
You J.
Xue H.
Chao C.
Zhang Z.
Tan X.
Wang X.
Li H.
Environmental Toxicology, 2024, 39 (11) : 4974 - 4983
[37] The histone methyltransferase Suv39h1 increases class switch recombination specifically to IgA
Stavnezer, Janet
Bradley, Sean P.
Koulnis, Miroslav
Peters, Antoine H. F. M.
Jenuwein, Thomas
Schmidt, Madelyn
JOURNAL OF IMMUNOLOGY, 2006, 176 : S233 - S233
[38] The histone methyltransferase Suv39h1 increases class switch recombination specifically to IgA
Bradley, Sean P.
Kaminski, Denise A.
Peters, Antoine H. F. M.
Jenuwein, Thomas
Stavnezer, Janet
JOURNAL OF IMMUNOLOGY, 2006, 177 (02): : 1179 - 1188
[39] A two-state activation mechanism controls the histone methyltransferase Suv39h1
Mueller, Manuel M.
Fierz, Beat
Bittova, Lenka
Liszczak, Glen
Muir, Tom W.
NATURE CHEMICAL BIOLOGY, 2016, 12 (03) : 188 - 193
[40] Chaetocin disrupts the SUV39H1-HP1 interaction independent of SUV39H1 methyltransferase activity
Han, Linna
Lee, Jessica B.
Indermaur, Elaine W.
Keung, Albert J.
BIOCHEMICAL JOURNAL, 2023, 480 (06) : 421 - 432

← 1 2 3 4 5 →