{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,17]],"date-time":"2026-10-17T12:15:13Z","timestamp":1792239313181,"version":"4.4.0"},"reference-count":95,"publisher":"MDPI AG","issue":"7","license":[{"start":{"date-parts":[[2021,7,16]],"date-time":"2021-07-16T00:00:00Z","timestamp":1626393600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100001659","name":"Deutsche Forschungsgemeinschaft","doi-asserted-by":"publisher","award":["JE 252\/7-4"],"award-info":[{"award-number":["JE 252\/7-4"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100007948","name":"Deutscher Akademischer Austausch Dienst Kairo","doi-asserted-by":"publisher","award":["GERLS scholarship number 57311832"],"award-info":[{"award-number":["GERLS scholarship number 57311832"]}],"id":[{"id":"10.13039\/501100007948","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003008","name":"Ministry of Higher Education, Egypt","doi-asserted-by":"publisher","award":["GERLS scholarship number 57311832"],"award-info":[{"award-number":["GERLS scholarship number 57311832"]}],"id":[{"id":"10.13039\/501100003008","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Life"],"abstract":"<jats:p>SUV39H1 and SUV39H2 were the first protein lysine methyltransferases that were identified more than 20 years ago. Both enzymes introduce di- and trimethylation at histone H3 lysine 9 (H3K9) and have important roles in the maintenance of heterochromatin and gene repression. They consist of a catalytically active SET domain and a chromodomain, which binds H3K9me2\/3 and has roles in enzyme targeting and regulation. The heterochromatic targeting of SUV39H enzymes is further enhanced by the interaction with HP1 proteins and repeat-associated RNA. SUV39H1 and SUV39H2 recognize an RKST motif with additional residues on both sides, mainly K4 in the case of SUV39H1 and G12 in the case of SUV39H2. Both SUV39H enzymes methylate different non-histone proteins including RAG2, DOT1L, SET8 and HupB in the case of SUV39H1 and LSD1 in the case of SUV39H2. Both enzymes are expressed in embryonic cells and have broad expression profiles in the adult body. SUV39H1 shows little tissue preference except thymus, while SUV39H2 is more highly expressed in the brain, testis and thymus. Both enzymes are connected to cancer, having oncogenic or tumor-suppressive roles depending on the tumor type. In addition, SUV39H2 has roles in the brain during early neurodevelopment.<\/jats:p>","DOI":"10.3390\/life11070703","type":"journal-article","created":{"date-parts":[[2021,7,18]],"date-time":"2021-07-18T21:16:48Z","timestamp":1626643008000},"page":"703","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":47,"title":["Structure, Activity and Function of the Suv39h1 and Suv39h2 Protein Lysine Methyltransferases"],"prefix":"10.3390","volume":"11","author":[{"given":"Sara","family":"Weirich","sequence":"first","affiliation":[{"name":"Institute of Biochemistry and Technical Biochemistry, University of Stuttgart, Allmandring 31, 70569 Stuttgart, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2111-0375","authenticated-orcid":false,"given":"Mina S.","family":"Khella","sequence":"additional","affiliation":[{"name":"Institute of Biochemistry and Technical Biochemistry, University of Stuttgart, Allmandring 31, 70569 Stuttgart, Germany"},{"name":"Biochemistry Department, Faculty of Pharmacy, Ain Shams University, African Union Organization Street, Abbassia, Cairo 11566, Egypt"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6113-9290","authenticated-orcid":false,"given":"Albert","family":"Jeltsch","sequence":"additional","affiliation":[{"name":"Institute of Biochemistry and Technical Biochemistry, University of Stuttgart, Allmandring 31, 70569 Stuttgart, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2021,7,16]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"693","DOI":"10.1016\/j.cell.2007.02.005","article-title":"Chromatin Modifications and Their Function","volume":"128","author":"Kouzarides","year":"2007","journal-title":"Cell"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"1016","DOI":"10.1016\/j.cell.2011.08.008","article-title":"Identification of 67 Histone Marks and Histone Lysine Crotonylation as a New Type of Histone Modification","volume":"146","author":"Tan","year":"2011","journal-title":"Cell"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"285","DOI":"10.1038\/nrg2752","article-title":"Chromatin structure and the inheritance of epigenetic information","volume":"11","author":"Margueron","year":"2010","journal-title":"Nat. Rev. Genet."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"381","DOI":"10.1038\/cr.2011.22","article-title":"Regulation of chromatin by histone modifications","volume":"21","author":"Bannister","year":"2011","journal-title":"Cell Res."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"1567","DOI":"10.1126\/science.1230184","article-title":"Epigenetic Reprogramming in Cancer","volume":"339","author":"Riggi","year":"2013","journal-title":"Science"},{"key":"ref_6","first-page":"366","article-title":"Role of somatic cancer mutations in human protein lysine methyltransferases","volume":"1846","author":"Kudithipudi","year":"2014","journal-title":"Biochim. Biophys. Acta (BBA) Bioenerg."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"838","DOI":"10.1038\/nrm1761","article-title":"The diverse functions of histone lysine methylation","volume":"6","author":"Martin","year":"2005","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"254","DOI":"10.1002\/cbic.201000545","article-title":"Structure and Function of Histone H3 Lysine 9 Methyltransferases and Demethylases","volume":"12","author":"Krishnan","year":"2011","journal-title":"ChemBioChem"},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1016\/j.tig.2015.11.001","article-title":"H3K9me3-Dependent Heterochromatin: Barrier to Cell Fate Changes","volume":"32","author":"Becker","year":"2016","journal-title":"Trends Genet."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"499","DOI":"10.1038\/nrm4029","article-title":"Sound of silence: The properties and functions of repressive Lys methyltransferases","volume":"16","author":"Mozzetta","year":"2015","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"823","DOI":"10.1016\/j.cell.2007.05.009","article-title":"High-Resolution Profiling of Histone Methylations in the Human Genome","volume":"129","author":"Barski","year":"2007","journal-title":"Cell"},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"3822","DOI":"10.1002\/j.1460-2075.1994.tb06693.x","article-title":"The protein encoded by the Drosophila posi-tion-effect variegation suppressor gene Su(var)3-9 combines domains of antagonistic regulators of homeotic gene com-plexes","volume":"13","author":"Tschiersch","year":"1994","journal-title":"EMBO J."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"593","DOI":"10.1038\/35020506","article-title":"Regulation of chromatin structure by site-specific histone H3 methyltransferases","volume":"406","author":"Rea","year":"2000","journal-title":"Nature"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"9423","DOI":"10.1128\/MCB.20.24.9423-9433.2000","article-title":"Isolation and Characterization of Suv39h2, a Second Histone H3 Methyltransferase Gene That Displays Testis-Specific Expression","volume":"20","author":"Scherthan","year":"2000","journal-title":"Mol. Cell. Biol."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"110","DOI":"10.1126\/science.1060118","article-title":"Role of Histone H3 Lysine 9 Methylation in Epigenetic Control of Heterochromatin Assembly","volume":"292","author":"Nakayama","year":"2001","journal-title":"Science"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"149","DOI":"10.1023\/A:1022923508198","article-title":"SU(VAR)3-9 is a Conserved Key Function in Heterochromatic Gene Silencing","volume":"117","author":"Schotta","year":"2003","journal-title":"Genetica"},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"267","DOI":"10.1146\/annurev.biophys.34.040204.144452","article-title":"Structural and Sequence Motifs of Protein (Histone) Methylation Enzymes","volume":"34","author":"Cheng","year":"2005","journal-title":"Annu. Rev. Biophys. Biomol. Struct."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"227","DOI":"10.1186\/gb-2005-6-8-227","article-title":"The SET-domain protein superfamily: Protein lysine methyltransferases","volume":"6","author":"Dillon","year":"2005","journal-title":"Genome Biol."},{"key":"ref_19","doi-asserted-by":"crossref","unstructured":"Wu, H., Min, J., Lunin, V.V., Antoshenko, T., Dombrovski, L., Zeng, H., Allali-Hassani, A., Campagna-Slater, V., Vedadi, M., and Arrowsmith, C. (2010). Structural Biology of Human H3K9 Methyltransferases. PLoS ONE, 5.","DOI":"10.1371\/journal.pone.0008570"},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"1025","DOI":"10.1038\/nsmb1338","article-title":"How chromatin-binding modules interpret histone modifications: Lessons from professional pocket pickers","volume":"14","author":"Taverna","year":"2007","journal-title":"Nat. Struct. Mol. Biol."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1146\/annurev-biochem-072711-165700","article-title":"Readout of Epigenetic Modifications","volume":"82","author":"Patel","year":"2013","journal-title":"Annu. Rev. Biochem."},{"key":"ref_22","doi-asserted-by":"crossref","unstructured":"Wang, T., Xu, C., Liu, Y., Fan, K., Li, Z., Sun, X., Ouyang, H., Zhang, X., Zhang, J., and Li, Y. (2012). Crystal Structure of the Human SUV39H1 Chromodomain and Its Recognition of Histone H3K9me2\/3. PLoS ONE, 7.","DOI":"10.1371\/journal.pone.0052977"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"6656","DOI":"10.1021\/acs.chemrev.8b00008","article-title":"Chemical and Biochemical Perspectives of Protein Lysine Methylation","volume":"118","author":"Luo","year":"2018","journal-title":"Chem. Rev."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"1577","DOI":"10.1016\/S1097-2765(03)00477-5","article-title":"Partitioning and Plasticity of Repressive Histone Methylation States in Mammalian Chromatin","volume":"12","author":"Peters","year":"2003","journal-title":"Mol. Cell"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"3272","DOI":"10.1021\/bi051997r","article-title":"Catalytic Properties and Kinetic Mechanism of Human Recombinant Lys-9 Histone H3 Methyltransferase SUV39H1: Participation of the Chromodomain in Enzymatic Catalysis","volume":"45","author":"Chin","year":"2006","journal-title":"Biochemistry"},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"958","DOI":"10.1021\/acschembio.6b01076","article-title":"The SUV39H1 Protein Lysine Methyltransferase Methylates Chromatin Proteins Involved in Heterochromatin Formation and VDJ Recombination","volume":"12","author":"Kudithipudi","year":"2017","journal-title":"ACS Chem. Biol."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"344","DOI":"10.1038\/nchembio.88","article-title":"Protein lysine methyltransferase G9a acts on non-histone targets","volume":"4","author":"Rathert","year":"2008","journal-title":"Nat. Chem. Biol."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1016\/j.bbagrm.2014.11.005","article-title":"Activity and specificity of the human SUV39H2 protein lysine methyltransferase","volume":"1849","author":"Schuhmacher","year":"2015","journal-title":"Biochim. Biophys. Acta (BBA) Bioenerg."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"479","DOI":"10.1101\/gad.967202","article-title":"Set9, a novel histone H3 methyltransferase that facilitates transcription by precluding histone tail modifications required for heterochromatin formation","volume":"16","author":"Nishioka","year":"2002","journal-title":"Genes Dev."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"767","DOI":"10.4161\/epi.5.8.13278","article-title":"Trimethylation of histone H3 lysine 4 impairs meth-ylation of histone H3 lysine 9: Regulation of lysine methyltransferases by physical interaction with their substrates","volume":"5","author":"Binda","year":"2010","journal-title":"Epigenetics"},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"1188","DOI":"10.1101\/gr.849004","article-title":"WebLogo: A Sequence Logo Generator","volume":"14","author":"Crooks","year":"2004","journal-title":"Genome Res."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"1591","DOI":"10.1016\/S1097-2765(03)00479-9","article-title":"Histone Methyltransferases Direct Different Degrees of Methylation to Define Distinct Chromatin Domains","volume":"12","author":"Rice","year":"2003","journal-title":"Mol. Cell"},{"key":"ref_33","first-page":"71","article-title":"Fluorescence-Based Methods for Screening Writers and Readers of Histone Methyl Marks","volume":"17","author":"Wasney","year":"2011","journal-title":"J. Biomol. Screen."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"5","DOI":"10.1016\/j.chembiol.2007.11.013","article-title":"Analysis of the Substrate Specificity of the Dim-5 Histone Lysine Methyltransferase Using Peptide Arrays","volume":"15","author":"Rathert","year":"2008","journal-title":"Chem. Biol."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"2344","DOI":"10.1016\/j.jmb.2016.04.015","article-title":"Specificity of the SUV4\u201320H1 and SUV4\u201320H2 protein lysine methyltransferases and methylation of novel substrates","volume":"428","author":"Weirich","year":"2016","journal-title":"J. Mol. Biol."},{"key":"ref_36","first-page":"504","article-title":"Automethylation-induced conformational switch in Clr4 (Suv39h) maintains epigenetic stability","volume":"560","author":"Iglesias","year":"2018","journal-title":"Nat. Cell Biol."},{"key":"ref_37","doi-asserted-by":"crossref","unstructured":"Khella, M.S., Br\u00f6hm, A., Weirich, S., and Jeltsch, A. (2020). Mechanistic Insights into the Allosteric Regulation of the Clr4 Protein Lysine Methyltransferase by Autoinhibition and Automethylation. Int. J. Mol. Sci., 21.","DOI":"10.3390\/ijms21228832"},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"22846","DOI":"10.18632\/oncotarget.8072","article-title":"Automethylation of SUV39H2, an oncogenic histone lysine methyltransferase, regulates its binding affinity to substrate proteins","volume":"7","author":"Piao","year":"2016","journal-title":"Oncotarget"},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"188","DOI":"10.1038\/nchembio.2008","article-title":"A two-state activation mechanism controls the histone methyltransferase Suv39h1","volume":"12","author":"Fierz","year":"2016","journal-title":"Nat. Chem. Biol."},{"key":"ref_40","doi-asserted-by":"crossref","unstructured":"Johnson, W.L., Yewdell, W.T., Bell, J.C., McNulty, S., Duda, Z., O\u2019Neill, R.J., Sullivan, B.A., and Straight, A.F. (2017). RNA-dependent stabilization of SUV39H1 at constitutive heterochromatin. eLife, 6.","DOI":"10.7554\/eLife.25299"},{"key":"ref_41","first-page":"6","article-title":"Impact of nucleic acid and methylated H3K9 binding activities of Suv39h1 on its heterochromatin assembly","volume":"6","author":"Shirai","year":"2017","journal-title":"eLife"},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"5379","DOI":"10.1038\/ncomms6379","article-title":"Functional characterization of the TERRA transcriptome at damaged telomeres","volume":"5","author":"Porro","year":"2014","journal-title":"Nat. Commun."},{"key":"ref_43","first-page":"120","article-title":"Selective recognition of methylated lysine 9 on histone H3 by the HP1 chromo domain","volume":"410","author":"Bannister","year":"2001","journal-title":"Nat. Cell Biol."},{"key":"ref_44","first-page":"116","article-title":"Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins","volume":"410","author":"Lachner","year":"2001","journal-title":"Nat. Cell Biol."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"287","DOI":"10.1016\/S0006-291X(02)03021-8","article-title":"Self-interaction of heterochromatin protein 1 is required for direct binding to histone methyltransferase, SUV39H1","volume":"301","author":"Yamamoto","year":"2003","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"145","DOI":"10.1247\/csf.16013","article-title":"Pericentric H3K9me3 formation by HP1 interaction-defective histone methyltransferase Suv39h1","volume":"41","author":"Muramatsu","year":"2016","journal-title":"Cell Struct. Funct."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"5516","DOI":"10.1073\/pnas.1216596110","article-title":"Methylation of SUV39H1 by SET7\/9 results in heterochromatin relaxation and genome instability","volume":"110","author":"Wang","year":"2013","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"970","DOI":"10.1016\/j.stemcr.2016.05.007","article-title":"Age-Associated Decrease of the Histone Methyltransferase SUV39H1 in HSC Perturbs Heterochromatin and B Lymphoid Differentiation","volume":"6","author":"Djeghloul","year":"2016","journal-title":"Stem Cell Rep."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"70","DOI":"10.1093\/abbs\/gmr109","article-title":"Targeting protein lysine methylation and demethylation in cancers","volume":"44","author":"He","year":"2011","journal-title":"Acta Biochim. Biophys. Sin."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"1351","DOI":"10.1038\/onc.2012.169","article-title":"Interaction with Suv39H1 is critical for Snail-mediated E-cadherin repression in breast cancer","volume":"32","author":"Dong","year":"2013","journal-title":"Oncogene"},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"721","DOI":"10.7150\/jca.28254","article-title":"The Oncogenic Potential of SUV39H2: A Comprehensive and Perspective View","volume":"10","author":"Li","year":"2019","journal-title":"J. Cancer"},{"key":"ref_52","first-page":"231","article-title":"Suppressor of Variegation 3-9 Homolog 2, a Novel Binding Protein of Translationally Controlled Tumor Protein, Regulates Cancer Cell Proliferation","volume":"27","author":"Kim","year":"2019","journal-title":"Biomol. Ther."},{"key":"ref_53","first-page":"1846","article-title":"Tissue-based map of the human proteome","volume":"347","author":"Fagerberg","year":"2015","journal-title":"Science"},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"323","DOI":"10.1016\/S0092-8674(01)00542-6","article-title":"Loss of the Suv39h Histone Methyltransferases Impairs Mammalian Heterochromatin and Genome Stability","volume":"107","author":"Peters","year":"2001","journal-title":"Cell"},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1038\/ng789","article-title":"Histone H3 lysine 9 methylation is an epigenetic imprint of facultative heterochromatin","volume":"30","author":"Peters","year":"2001","journal-title":"Nat. Genet."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1016\/j.molcel.2014.05.029","article-title":"Suv39h-Dependent H3K9me3 Marks Intact Retrotransposons and Silences LINE Elements in Mouse Embryonic Stem Cells","volume":"55","author":"Ramirez","year":"2014","journal-title":"Mol. Cell"},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"2797","DOI":"10.1093\/nar\/gkt012","article-title":"Histone H4 Lysine 20 methylation: Key player in epigenetic regulation of genomic integrity","volume":"41","author":"Schotta","year":"2013","journal-title":"Nucleic Acids Res."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"1251","DOI":"10.1101\/gad.300704","article-title":"A silencing pathway to induce H3-K9 and H4-K20 trimethylation at constitutive heterochromatin","volume":"18","author":"Schotta","year":"2004","journal-title":"Genes Dev."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"2048","DOI":"10.1101\/gad.476008","article-title":"A chromatin-wide transition to H4K20 monomethylation impairs genome integrity and programmed DNA rearrangements in the mouse","volume":"22","author":"Schotta","year":"2008","journal-title":"Genes Dev."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"46","DOI":"10.1016\/j.molcel.2009.12.017","article-title":"A Subset of the Histone H3 Lysine 9 Methyltransferases Suv39h1, G9a, GLP, and SETDB1 Participate in a Multimeric Complex","volume":"37","author":"Fritsch","year":"2010","journal-title":"Mol. Cell"},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"1201","DOI":"10.1016\/S1097-2765(02)00548-8","article-title":"PR-Set7 Is a Nucleosome-Specific Methyltransferase that Modifies Lysine 20 of Histone H4 and Is Associated with Silent Chromatin","volume":"9","author":"Nishioka","year":"2002","journal-title":"Mol. Cell"},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"1086","DOI":"10.1016\/S0960-9822(02)00924-7","article-title":"Purification and Functional Characterization of SET8, a Nucleosomal Histone H4-Lysine 20-Specific Methyltransferase","volume":"12","author":"Fang","year":"2002","journal-title":"Curr. Biol."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"2212","DOI":"10.1016\/j.biochi.2012.04.024","article-title":"The SET8 H4K20 protein lysine methyltransferase has a long recognition sequence covering seven amino acid residues","volume":"94","author":"Kudithipudi","year":"2012","journal-title":"Biochimie"},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"2278","DOI":"10.1128\/MCB.01768-08","article-title":"Monomethylation of Histone H4-Lysine 20 Is Involved in Chromosome Structure and Stability and Is Essential for Mouse Development","volume":"29","author":"Oda","year":"2009","journal-title":"Mol. Cell. Biol."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"1179","DOI":"10.4049\/jimmunol.177.2.1179","article-title":"The histone methyltransferase Suv39h1 increases class switch recombination specifically to IgA","volume":"177","author":"Bradley","year":"2006","journal-title":"J. Immunol."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"5288","DOI":"10.1073\/pnas.0901368106","article-title":"H3 trimethyl K9 and H3 acetyl K9 chromatin modifications are associated with class switch recombination","volume":"106","author":"Kuang","year":"2009","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"2131","DOI":"10.1038\/leu.2014.169","article-title":"The emerging roles of DOT1L in leukemia and normal development","volume":"28","author":"McLean","year":"2014","journal-title":"Leukemia"},{"key":"ref_68","doi-asserted-by":"crossref","unstructured":"Jones, B., Su, H., Bhat, A., Lei, H., Bajko, J., Hevi, S., Baltus, G.A., Kadam, S., Zhai, H., and Valdez, R. (2008). The Histone H3K79 Methyltransferase Dot1L Is Essential for Mammalian Development and Heterochromatin Structure. PLoS Genet., 4.","DOI":"10.1371\/journal.pgen.1000190"},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"183","DOI":"10.15252\/embj.201796918","article-title":"Histone methyltransferase SUV 39H1 participates in host defense by methylating mycobacterial histone-like protein HupB","volume":"37","author":"Yaseen","year":"2018","journal-title":"EMBO J."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"16939","DOI":"10.18632\/oncotarget.4760","article-title":"SUV39H2 methylates and stabilizes LSD1 by inhibiting polyubiquitination in human cancer cells","volume":"6","author":"Piao","year":"2015","journal-title":"Oncotarget"},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"5691","DOI":"10.1038\/ncomms6691","article-title":"Critical role of lysine 134 methylation on histone H2AX for \u03b3-H2AX production and DNA repair","volume":"5","author":"Sone","year":"2014","journal-title":"Nat. Commun."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"1713","DOI":"10.1002\/1873-3468.12216","article-title":"Investigation of H2AX methylation by the SUV39H2 protein lysine methyltransferase","volume":"590","author":"Schuhmacher","year":"2016","journal-title":"FEBS Lett."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"593","DOI":"10.1126\/science.1200801","article-title":"Aberrant Overexpression of Satellite Repeats in Pancreatic and Other Epithelial Cancers","volume":"331","author":"Ting","year":"2011","journal-title":"Science"},{"key":"ref_74","first-page":"179","article-title":"BRCA1 tumour suppression occurs via heterochromatin-mediated silencing","volume":"477","author":"Zhu","year":"2011","journal-title":"Nat. Cell Biol."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"7931","DOI":"10.1093\/nar\/gkv722","article-title":"SETDB1, HP1 and SUV39 promote repositioning of 53BP1 to extend resection during homologous recombination in G2 cells","volume":"43","author":"Alagoz","year":"2015","journal-title":"Nucleic Acids Res."},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"9169","DOI":"10.1073\/pnas.1403565111","article-title":"DNA double-strand breaks promote methylation of histone H3 on lysine 9 and transient formation of repressive chromatin","volume":"111","author":"Ayrapetov","year":"2014","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"734","DOI":"10.1038\/onc.2013.6","article-title":"p53 promotes repair of heterochromatin DNA by regulating JMJD2b and SUV39H1 expression","volume":"33","author":"Zheng","year":"2013","journal-title":"Oncogene"},{"key":"ref_78","first-page":"94","article-title":"Epigenetic regulation of telomere length in mammalian cells by the Suv39h1 and Suv39h2 histone methyltransferases","volume":"36","author":"Peters","year":"2003","journal-title":"Nat. Genet."},{"key":"ref_79","first-page":"249","article-title":"An epigenetic silencing pathway controlling T helper 2 cell lineage commitment","volume":"487","author":"Allan","year":"2012","journal-title":"Nat. Cell Biol."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"7631","DOI":"10.1038\/ncomms8631","article-title":"Epigenetic silencing of Oct4 by a complex containing SUV39H1 and Oct4 pseudogene lncRNA","volume":"6","author":"Scarola","year":"2015","journal-title":"Nat. Commun."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"1160","DOI":"10.1126\/science.aaa1356","article-title":"A Werner syndrome stem cell model unveils heterochromatin alterations as a driver of human aging","volume":"348","author":"Zhang","year":"2015","journal-title":"Science"},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"7239","DOI":"10.1038\/s41388-020-01495-6","article-title":"SUV39H1 regulates the progression of MLL-AF9-induced acute myeloid leukemia","volume":"39","author":"Chu","year":"2020","journal-title":"Oncogene"},{"key":"ref_83","first-page":"660","article-title":"Oncogene-induced senescence as an initial barrier in lymphoma development","volume":"436","author":"Braig","year":"2005","journal-title":"Nat. Cell Biol."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"262","DOI":"10.1016\/j.ccr.2009.12.043","article-title":"Tumor Stroma-Derived TGF-\u03b2 Limits Myc-Driven Lymphomagenesis via Suv39h1-Dependent Senescence","volume":"17","author":"Reimann","year":"2010","journal-title":"Cancer Cell"},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"382","DOI":"10.1093\/nar\/gkp991","article-title":"The tumor suppressor, parafibromin, mediates histone H3 K9 methylation for cyclin D1 repression","volume":"38","author":"Yang","year":"2009","journal-title":"Nucleic Acids Res."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1186\/s13148-018-0562-4","article-title":"Identification of SUV39H2 as a potential oncogene in lung adenocarcinoma","volume":"10","author":"Zheng","year":"2018","journal-title":"Clin. Epigenetics"},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"368","DOI":"10.1016\/j.tranon.2015.07.003","article-title":"Targeting Suppressor of Variegation 3-9 Homologue 2 (SUV39H2) in Acute Lymphoblastic Leukemia (ALL)","volume":"8","author":"Mutonga","year":"2015","journal-title":"Transl. Oncol."},{"key":"ref_88","first-page":"325","article-title":"Histone methyltransferase SUV39H2 serves oncogenic roles in osteosarcoma","volume":"41","author":"Piao","year":"2018","journal-title":"Oncol. Rep."},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"269","DOI":"10.1186\/s12935-019-0982-z","article-title":"Histone methyltransferase SUV39H2 regulates cell growth and chemosensitivity in glioma via regulation of hedgehog signaling","volume":"19","author":"Wang","year":"2019","journal-title":"Cancer Cell Int."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"373","DOI":"10.1002\/1878-0261.12041","article-title":"Somatic cancer mutations in the MLL1 histone methyltransferase modulate its enzymatic activity and dependence on the WDR5\/RBBP5\/ASH2L complex","volume":"11","author":"Weirich","year":"2017","journal-title":"Mol. Oncol."},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"56","DOI":"10.1016\/j.canlet.2018.02.023","article-title":"SUV39H2 promotes colorectal cancer proliferation and metastasis via tri-methylation of the SLIT1 promoter","volume":"422","author":"Shuai","year":"2018","journal-title":"Cancer Lett."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"17657","DOI":"10.1073\/pnas.1215810109","article-title":"Acute stress and hippocampal histone H3 lysine 9 trimethylation, a retrotransposon silencing response","volume":"109","author":"Hunter","year":"2012","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_93","doi-asserted-by":"crossref","unstructured":"Balan, S., Iwayama, Y., Ohnishi, T., Fukuda, M., Shirai, A., Yamada, A., Weirich, S., Schuhmacher, M.K., Vijayan, D.K., and Endo, T. (2021). A loss of function variant in SUV39H2 identified in autism spectrum disorder causes altered H3K9-trimethylation and dysregulation of protocadherin \u03b2 cluster genes in the developing brain. Mol. Psychiatry.","DOI":"10.1038\/s41380-021-01199-7"},{"key":"ref_94","doi-asserted-by":"crossref","unstructured":"Jagannathan, V., Bannoehr, J., Plattet, P., Hauswirth, R., Dr\u00f6gem\u00fcller, C., Dr\u00f6gem\u00fcller, M., Wiener, D.J., Doherr, M., Owczarek-Lipska, M., and Galichet, A. (2013). A Mutation in the SUV39H2 Gene in Labrador Retrievers with Hereditary Nasal Parakeratosis (HNPK) Provides Insights into the Epigenetics of Keratinocyte Differentiation. PLoS Genet., 9.","DOI":"10.1371\/journal.pgen.1003848"},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"884","DOI":"10.1016\/j.celrep.2014.10.001","article-title":"Heterochromatin-Mediated Gene Silencing Facilitates the Diversification of Olfactory Neurons","volume":"9","author":"Lyons","year":"2014","journal-title":"Cell Rep."}],"container-title":["Life"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2075-1729\/11\/7\/703\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T06:31:05Z","timestamp":1760164265000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2075-1729\/11\/7\/703"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,7,16]]},"references-count":95,"journal-issue":{"issue":"7","published-online":{"date-parts":[[2021,7]]}},"alternative-id":["life11070703"],"URL":"https:\/\/doi.org\/10.3390\/life11070703","relation":{},"ISSN":["2075-1729"],"issn-type":[{"value":"2075-1729","type":"electronic"}],"subject":[],"published":{"date-parts":[[2021,7,16]]}}}