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A cluster of genes, BAT1-BAT5, has been localized in the vicinity of the genes for TNF alpha and TNF beta. This gene is found near this cluster; it was mapped near the gene for C2 within a 120-kb region that included a HSP70 gene pair. These genes are all within the human major histocompatibility complex class III region. This gene was thought to be two different genes, NG36 and G9a, adjacent to each other but a recent publication shows that there is only a single gene. The protein encoded by this gene is thought to be involved in intracellular protein-protein interaction. There are three alternatively spliced transcript variants of this gene but only two are fully described.<ref name="entrez"/> |
A cluster of genes, BAT1-BAT5, has been localized in the vicinity of the genes for TNF alpha and TNF beta. This gene is found near this cluster; it was mapped near the gene for C2 within a 120-kb region that included a HSP70 gene pair. These genes are all within the human major histocompatibility complex class III region. This gene was thought to be two different genes, NG36 and G9a, adjacent to each other but a recent publication shows that there is only a single gene. The protein encoded by this gene is thought to be involved in intracellular protein-protein interaction. There are three alternatively spliced transcript variants of this gene but only two are fully described.<ref name="entrez"/> |
||
G9a and [[G9a-like protein]], another histone-lysine N-methyltransferase, catalyze the synthesis of [[H3K9me2]], which is a [[repressor|repressive]] mark.<ref name="pmid26472529" /><ref name="Histome G9a">{{cite web |title=Histone-lysine N-methyltransferase, H3 lysine-9 specific 3 |url=http://www.actrec.gov.in/histome/enzyme_sp.php?enzyme_sp=Histone-lysine_N-methyltransferase,_H3_lysine-9_specific_3 |publisher=HIstome: The Histone Infobase |accessdate=8 June 2018|quote=}}</ref><ref name="Histome GLP">{{cite web |title=Histone-lysine N-methyltransferase, H3 lysine-9 specific 5 |url=http://www.actrec.gov.in/histome/enzyme_sp.php?enzyme_sp=Histone-lysine_N-methyltransferase,_H3_lysine-9_specific_5 |publisher=HIstome: The Histone Infobase |accessdate=8 June 2018}}</ref> G9a is an important control mechanism for [[epigenetic regulation]] within the [[nucleus accumbens]] (NAcc);<ref name="Nestler 2014 epigenetics" /> reduced G9a expression in the NAcc plays a central role in mediating the development of an [[addiction]].<ref name="Nestler 2014 epigenetics" /> G9a opposes increases in [[ΔFosB]] expression via [[H3K9me2]] and is suppressed by ΔFosB.<ref name="Nestler 2014 epigenetics" /> G9a exerts opposite effects to that of ΔFosB on drug-related behavior (e.g., [[self-administration]]) and synaptic remodeling (e.g., [[dendritic arborization]] – the development of additional tree-like [[dendrite|dendritic branches]] and [[dendritic spine|spines]]) in the nucleus accumbens, and therefore opposes ΔFosB's function as well as increases in its expression.<ref name="Nestler 2014 epigenetics">{{cite journal | vauthors = Nestler EJ | title = Epigenetic mechanisms of drug addiction | journal = Neuropharmacology | volume = 76 Pt B | issue = | pages = 259–268 | date = January 2014 | pmid = 23643695 | pmc = 3766384 | doi = 10.1016/j.neuropharm.2013.04.004 | quote = Short-term increases in histone acetylation generally promote behavioral responses to the drugs, while sustained increases oppose cocaine’s effects, based on the actions of systemic or intra-NAc administration of HDAC inhibitors. ... Genetic or pharmacological blockade of G9a in the NAc potentiates behavioral responses to cocaine and opiates, whereas increasing G9a function exerts the opposite effect (Maze et al., 2010; Sun et al., 2012a). Such drug-induced downregulation of G9a and H3K9me2 also sensitizes animals to the deleterious effects of subsequent chronic stress (Covington et al., 2011). Downregulation of G9a increases the dendritic arborization of NAc neurons, and is associated with increased expression of numerous proteins implicated in synaptic function, which directly connects altered G9a/H3K9me2 in the synaptic plasticity associated with addiction (Maze et al., 2010).<br />G9a appears to be a critical control point for epigenetic regulation in NAc, as we know it functions in two negative feedback loops. It opposes the induction of ΔFosB, a long-lasting transcription factor important for drug addiction (Robison and Nestler, 2011), while ΔFosB in turn suppresses G9a expression (Maze et al., 2010; Sun et al., 2012a). ... Also, G9a is induced in NAc upon prolonged HDAC inhibition, which explains the paradoxical attenuation of cocaine’s behavioral effects seen under these conditions, as noted above (Kennedy et al., 2013). GABAA receptor subunit genes are among those that are controlled by this feedback loop. Thus, chronic cocaine, or prolonged HDAC inhibition, induces several GABAA receptor subunits in NAc, which is associated with increased frequency of inhibitory postsynaptic currents (IPSCs). In striking contrast, combined exposure to cocaine and HDAC inhibition, which triggers the induction of G9a and increased global levels of H3K9me2, leads to blockade of GABAA receptor and IPSC regulation. }}</ref> G9a and ΔFosB share many of the same gene targets.<ref name="Nestler1">{{cite journal | author = Robison AJ, Nestler EJ | title = Transcriptional and epigenetic mechanisms of addiction | journal = Nat. Rev. Neurosci. | volume = 12 | issue = 11 | pages = 623–637 | date = November 2011 | pmid = 21989194 | pmc = 3272277 | doi = 10.1038/nrn3111 | quote = ΔFosB serves as one of the master control proteins governing this structural plasticity. ... ΔFosB also represses G9a expression, leading to reduced repressive histone methylation at the cdk5 gene. The net result is gene activation and increased CDK5 expression. ... In contrast, ΔFosB binds to the c-fos gene and recruits several co-repressors, including HDAC1 (histone deacetylase 1) and SIRT 1 (sirtuin 1). ... The net result is c-fos gene repression. ... G9a and ΔFosB share many of the same target genes.}}<br />[https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3272277/figure/F4/ Figure 4: Epigenetic basis of drug regulation of gene expression]</ref> |
G9a and [[G9a-like protein]], another histone-lysine N-methyltransferase, catalyze the synthesis of [[H3K9me2]], which is a [[repressor|repressive]] mark.<ref name="pmid26472529" /><ref name="Histome G9a">{{cite web |title=Histone-lysine N-methyltransferase, H3 lysine-9 specific 3 |url=http://www.actrec.gov.in/histome/enzyme_sp.php?enzyme_sp=Histone-lysine_N-methyltransferase,_H3_lysine-9_specific_3 |publisher=HIstome: The Histone Infobase |accessdate=8 June 2018|quote=}}</ref><ref name="Histome GLP">{{cite web |title=Histone-lysine N-methyltransferase, H3 lysine-9 specific 5 |url=http://www.actrec.gov.in/histome/enzyme_sp.php?enzyme_sp=Histone-lysine_N-methyltransferase,_H3_lysine-9_specific_5 |publisher=HIstome: The Histone Infobase |accessdate=8 June 2018}}</ref> G9a is an important control mechanism for [[epigenetic regulation]] within the [[nucleus accumbens]] (NAcc);<ref name="Nestler 2014 epigenetics" /> reduced G9a expression in the NAcc plays a central role in mediating the development of an [[addiction]].<ref name="Nestler 2014 epigenetics" /> G9a opposes increases in [[ΔFosB]] expression via [[H3K9me2]] and is suppressed by ΔFosB.<ref name="Nestler 2014 epigenetics" /> G9a exerts opposite effects to that of ΔFosB on drug-related behavior (e.g., [[self-administration]]) and synaptic remodeling (e.g., [[dendritic arborization]] – the development of additional tree-like [[dendrite|dendritic branches]] and [[dendritic spine|spines]]) in the nucleus accumbens, and therefore opposes ΔFosB's function as well as increases in its expression.<ref name="Nestler 2014 epigenetics">{{cite journal | vauthors = Nestler EJ | title = Epigenetic mechanisms of drug addiction | journal = Neuropharmacology | volume = 76 Pt B | issue = | pages = 259–268 | date = January 2014 | pmid = 23643695 | pmc = 3766384 | doi = 10.1016/j.neuropharm.2013.04.004 | quote = Short-term increases in histone acetylation generally promote behavioral responses to the drugs, while sustained increases oppose cocaine’s effects, based on the actions of systemic or intra-NAc administration of HDAC inhibitors. ... Genetic or pharmacological blockade of G9a in the NAc potentiates behavioral responses to cocaine and opiates, whereas increasing G9a function exerts the opposite effect (Maze et al., 2010; Sun et al., 2012a). Such drug-induced downregulation of G9a and H3K9me2 also sensitizes animals to the deleterious effects of subsequent chronic stress (Covington et al., 2011). Downregulation of G9a increases the dendritic arborization of NAc neurons, and is associated with increased expression of numerous proteins implicated in synaptic function, which directly connects altered G9a/H3K9me2 in the synaptic plasticity associated with addiction (Maze et al., 2010).<br />G9a appears to be a critical control point for epigenetic regulation in NAc, as we know it functions in two negative feedback loops. It opposes the induction of ΔFosB, a long-lasting transcription factor important for drug addiction (Robison and Nestler, 2011), while ΔFosB in turn suppresses G9a expression (Maze et al., 2010; Sun et al., 2012a). ... Also, G9a is induced in NAc upon prolonged HDAC inhibition, which explains the paradoxical attenuation of cocaine’s behavioral effects seen under these conditions, as noted above (Kennedy et al., 2013). GABAA receptor subunit genes are among those that are controlled by this feedback loop. Thus, chronic cocaine, or prolonged HDAC inhibition, induces several GABAA receptor subunits in NAc, which is associated with increased frequency of inhibitory postsynaptic currents (IPSCs). In striking contrast, combined exposure to cocaine and HDAC inhibition, which triggers the induction of G9a and increased global levels of H3K9me2, leads to blockade of GABAA receptor and IPSC regulation. }}</ref> G9a and ΔFosB share many of the same gene targets.<ref name="Nestler1">{{cite journal | author = Robison AJ, Nestler EJ | title = Transcriptional and epigenetic mechanisms of addiction | journal = Nat. Rev. Neurosci. | volume = 12 | issue = 11 | pages = 623–637 | date = November 2011 | pmid = 21989194 | pmc = 3272277 | doi = 10.1038/nrn3111 | quote = ΔFosB serves as one of the master control proteins governing this structural plasticity. ... ΔFosB also represses G9a expression, leading to reduced repressive histone methylation at the cdk5 gene. The net result is gene activation and increased CDK5 expression. ... In contrast, ΔFosB binds to the c-fos gene and recruits several co-repressors, including HDAC1 (histone deacetylase 1) and SIRT 1 (sirtuin 1). ... The net result is c-fos gene repression. ... G9a and ΔFosB share many of the same target genes. ... Histone methylation is directly regulated by drugs of abuse as well: global levels of histone 3 lysine 9 dimethylation (H3K9me2) are reduced in the NAc after chronic cocaine37 and a genome-wide screen revealed alterations in H3K9me2 binding on the promoters of numerous genes in this brain region32; both increases and decreases were observed, indicating again that epigenetic modifications at individual genes often defy global changes. The global decrease in H3K9me2 in the NAc is likely mediated by cocaine-induced downregulation of two HMTs, G9a and G9a-like protein (GLP), which catalyze H3K9me2<sup>37</sup>. These adaptations mediate enhanced responsiveness to cocaine, as selective knockout or pharmacological inhibition of G9a in the NAc promotes cocaine-induced behaviors, whereas G9a overexpression has the opposite effect. G9a likewise mediates the ability of cocaine to increase the spine density of NAc MSNs<sup>37</sup> (Box 2). Interestingly, there is a functional feedback loop between G9a and ΔFosB: ΔFosB seems to be responsible for cocaine-induced suppression of G9a, and G9a binds to and represses the fosb promoter, such that G9a downregulation may promote the accumulation of ΔFosB observed after chronic cocaine37. In addition, G9a and ΔFosB share many of the same target genes. ... The mechanisms underlying such gene desensitization and priming remain incompletely understood; our hypothesis is that epigenetic mechanisms are crucial (Figure 3B). A subset of primed genes show reduced binding of G9a and H3K9me2 at their promoters in the NAc, suggesting the involvement of this epigenetic mark<sup>37</sup>. Desensitization of the c-fos gene in the NAc, discussed above and depicted in Figure 4, involves stable increases in the binding of ΔFosB, G9a, and related co-repressors, which—although not affecting steady-state levels of c-Fos mRNA—dramatically repress its inducibility to subsequent drug exposure<sup>91</sup>.}}<br />[https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3272277/figure/F4/ Figure 4: Epigenetic basis of drug regulation of gene expression]</ref> |
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== Interactions == |
== Interactions == |
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Revision as of 21:48, 23 June 2018
Euchromatic histone-lysine N-methyltransferase 2 (EHMT2), also known as G9a, is a histone methyltransferase that in humans is encoded by the EHMT2 gene.[5][6][7] G9a catalyzes the mono- and di-methylated states of histone H3 at lysine residue 9 (i.e., H3K9me1 and H3K9me2) and lysine residue 27 (H3K27me1 and HeK27me2).[8]
Function
A cluster of genes, BAT1-BAT5, has been localized in the vicinity of the genes for TNF alpha and TNF beta. This gene is found near this cluster; it was mapped near the gene for C2 within a 120-kb region that included a HSP70 gene pair. These genes are all within the human major histocompatibility complex class III region. This gene was thought to be two different genes, NG36 and G9a, adjacent to each other but a recent publication shows that there is only a single gene. The protein encoded by this gene is thought to be involved in intracellular protein-protein interaction. There are three alternatively spliced transcript variants of this gene but only two are fully described.[7]
G9a and G9a-like protein, another histone-lysine N-methyltransferase, catalyze the synthesis of H3K9me2, which is a repressive mark.[8][9][10] G9a is an important control mechanism for epigenetic regulation within the nucleus accumbens (NAcc);[11] reduced G9a expression in the NAcc plays a central role in mediating the development of an addiction.[11] G9a opposes increases in ΔFosB expression via H3K9me2 and is suppressed by ΔFosB.[11] G9a exerts opposite effects to that of ΔFosB on drug-related behavior (e.g., self-administration) and synaptic remodeling (e.g., dendritic arborization – the development of additional tree-like dendritic branches and spines) in the nucleus accumbens, and therefore opposes ΔFosB's function as well as increases in its expression.[11] G9a and ΔFosB share many of the same gene targets.[12]
Interactions
EHMT2 has been shown to interact with KIAA0515 and the prostate tissue associated homeodomain protein NKX3.1.[13][14]
References
- ^ a b c ENSG00000224143, ENSG00000206376, ENSG00000204371, ENSG00000227333, ENSG00000232045, ENSG00000236759 GRCh38: Ensembl release 89: ENSG00000238134, ENSG00000224143, ENSG00000206376, ENSG00000204371, ENSG00000227333, ENSG00000232045, ENSG00000236759 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000013787 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ Milner CM, Campbell RD (Mar 1993). "The G9a gene in the human major histocompatibility complex encodes a novel protein containing ankyrin-like repeats". The Biochemical Journal. 290 (Pt 3): 811–8. doi:10.1042/bj2900811. PMC 1132354. PMID 8457211.
- ^ Tachibana M, Sugimoto K, Fukushima T, Shinkai Y (Jul 2001). "Set domain-containing protein, G9a, is a novel lysine-preferring mammalian histone methyltransferase with hyperactivity and specific selectivity to lysines 9 and 27 of histone H3". The Journal of Biological Chemistry. 276 (27): 25309–17. doi:10.1074/jbc.M101914200. PMID 11316813.
{{cite journal}}: CS1 maint: unflagged free DOI (link) - ^ a b "Entrez Gene: EHMT2 euchromatic histone-lysine N-methyltransferase 2".
- ^ a b Nestler EJ (August 2015). "Role of the Brain's Reward Circuitry in Depression: Transcriptional Mechanisms". Int. Rev. Neurobiol. 124: 151–170. doi:10.1016/bs.irn.2015.07.003. PMC 4690450. PMID 26472529.
Chronic social defeat stress decreases expression of G9a and GLP (G9a-like protein), two histone methyltransferases that catalyze the dimethylation of Lys9 of histone H3 (H3K9me2) (Covington et al., 2011), a mark associated with gene repression.
- ^ "Histone-lysine N-methyltransferase, H3 lysine-9 specific 3". HIstome: The Histone Infobase. Retrieved 8 June 2018.
- ^ "Histone-lysine N-methyltransferase, H3 lysine-9 specific 5". HIstome: The Histone Infobase. Retrieved 8 June 2018.
- ^ a b c d Nestler EJ (January 2014). "Epigenetic mechanisms of drug addiction". Neuropharmacology. 76 Pt B: 259–268. doi:10.1016/j.neuropharm.2013.04.004. PMC 3766384. PMID 23643695.
Short-term increases in histone acetylation generally promote behavioral responses to the drugs, while sustained increases oppose cocaine's effects, based on the actions of systemic or intra-NAc administration of HDAC inhibitors. ... Genetic or pharmacological blockade of G9a in the NAc potentiates behavioral responses to cocaine and opiates, whereas increasing G9a function exerts the opposite effect (Maze et al., 2010; Sun et al., 2012a). Such drug-induced downregulation of G9a and H3K9me2 also sensitizes animals to the deleterious effects of subsequent chronic stress (Covington et al., 2011). Downregulation of G9a increases the dendritic arborization of NAc neurons, and is associated with increased expression of numerous proteins implicated in synaptic function, which directly connects altered G9a/H3K9me2 in the synaptic plasticity associated with addiction (Maze et al., 2010).
G9a appears to be a critical control point for epigenetic regulation in NAc, as we know it functions in two negative feedback loops. It opposes the induction of ΔFosB, a long-lasting transcription factor important for drug addiction (Robison and Nestler, 2011), while ΔFosB in turn suppresses G9a expression (Maze et al., 2010; Sun et al., 2012a). ... Also, G9a is induced in NAc upon prolonged HDAC inhibition, which explains the paradoxical attenuation of cocaine's behavioral effects seen under these conditions, as noted above (Kennedy et al., 2013). GABAA receptor subunit genes are among those that are controlled by this feedback loop. Thus, chronic cocaine, or prolonged HDAC inhibition, induces several GABAA receptor subunits in NAc, which is associated with increased frequency of inhibitory postsynaptic currents (IPSCs). In striking contrast, combined exposure to cocaine and HDAC inhibition, which triggers the induction of G9a and increased global levels of H3K9me2, leads to blockade of GABAA receptor and IPSC regulation. - ^ Robison AJ, Nestler EJ (November 2011). "Transcriptional and epigenetic mechanisms of addiction". Nat. Rev. Neurosci. 12 (11): 623–637. doi:10.1038/nrn3111. PMC 3272277. PMID 21989194.
ΔFosB serves as one of the master control proteins governing this structural plasticity. ... ΔFosB also represses G9a expression, leading to reduced repressive histone methylation at the cdk5 gene. The net result is gene activation and increased CDK5 expression. ... In contrast, ΔFosB binds to the c-fos gene and recruits several co-repressors, including HDAC1 (histone deacetylase 1) and SIRT 1 (sirtuin 1). ... The net result is c-fos gene repression. ... G9a and ΔFosB share many of the same target genes. ... Histone methylation is directly regulated by drugs of abuse as well: global levels of histone 3 lysine 9 dimethylation (H3K9me2) are reduced in the NAc after chronic cocaine37 and a genome-wide screen revealed alterations in H3K9me2 binding on the promoters of numerous genes in this brain region32; both increases and decreases were observed, indicating again that epigenetic modifications at individual genes often defy global changes. The global decrease in H3K9me2 in the NAc is likely mediated by cocaine-induced downregulation of two HMTs, G9a and G9a-like protein (GLP), which catalyze H3K9me237. These adaptations mediate enhanced responsiveness to cocaine, as selective knockout or pharmacological inhibition of G9a in the NAc promotes cocaine-induced behaviors, whereas G9a overexpression has the opposite effect. G9a likewise mediates the ability of cocaine to increase the spine density of NAc MSNs37 (Box 2). Interestingly, there is a functional feedback loop between G9a and ΔFosB: ΔFosB seems to be responsible for cocaine-induced suppression of G9a, and G9a binds to and represses the fosb promoter, such that G9a downregulation may promote the accumulation of ΔFosB observed after chronic cocaine37. In addition, G9a and ΔFosB share many of the same target genes. ... The mechanisms underlying such gene desensitization and priming remain incompletely understood; our hypothesis is that epigenetic mechanisms are crucial (Figure 3B). A subset of primed genes show reduced binding of G9a and H3K9me2 at their promoters in the NAc, suggesting the involvement of this epigenetic mark37. Desensitization of the c-fos gene in the NAc, discussed above and depicted in Figure 4, involves stable increases in the binding of ΔFosB, G9a, and related co-repressors, which—although not affecting steady-state levels of c-Fos mRNA—dramatically repress its inducibility to subsequent drug exposure91.
Figure 4: Epigenetic basis of drug regulation of gene expression - ^ Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (Oct 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
- ^ Dutta A, et al. (Jun 2016). "Identification of an NKX3.1-G9a-UTY transcriptional regulatory network that controls prostate differentiation". Science.
Further reading
- Spies T, Bresnahan M, Strominger JL (Nov 1989). "Human major histocompatibility complex contains a minimum of 19 genes between the complement cluster and HLA-B". Proceedings of the National Academy of Sciences of the United States of America. 86 (22): 8955–8. doi:10.1073/pnas.86.22.8955. PMC 298409. PMID 2813433.
- Brown SE, Campbell RD, Sanderson CM (Dec 2001). "Novel NG36/G9a gene products encoded within the human and mouse MHC class III regions". Mammalian Genome. 12 (12): 916–24. doi:10.1007/s00335-001-3029-3. PMID 11707778.
- Ogawa H, Ishiguro K, Gaubatz S, Livingston DM, Nakatani Y (May 2002). "A complex with chromatin modifiers that occupies E2F- and Myc-responsive genes in G0 cells". Science. 296 (5570): 1132–6. doi:10.1126/science.1069861. PMID 12004135.
- Tachibana M, Sugimoto K, Nozaki M, Ueda J, Ohta T, Ohki M, Fukuda M, Takeda N, Niida H, Kato H, Shinkai Y (Jul 2002). "G9a histone methyltransferase plays a dominant role in euchromatic histone H3 lysine 9 methylation and is essential for early embryogenesis". Genes & Development. 16 (14): 1779–91. doi:10.1101/gad.989402. PMC 186403. PMID 12130538.
- Shi Y, Sawada J, Sui G, Affar el B, Whetstine JR, Lan F, Ogawa H, Luke MP, Nakatani Y, Shi Y (Apr 2003). "Coordinated histone modifications mediated by a CtBP co-repressor complex". Nature. 422 (6933): 735–8. doi:10.1038/nature01550. PMID 12700765.
- Xie T, Rowen L, Aguado B, Ahearn ME, Madan A, Qin S, Campbell RD, Hood L (Dec 2003). "Analysis of the gene-dense major histocompatibility complex class III region and its comparison to mouse". Genome Research. 13 (12): 2621–36. doi:10.1101/gr.1736803. PMC 403804. PMID 14656967.
- Roopra A, Qazi R, Schoenike B, Daley TJ, Morrison JF (Jun 2004). "Localized domains of G9a-mediated histone methylation are required for silencing of neuronal genes". Molecular Cell. 14 (6): 727–38. doi:10.1016/j.molcel.2004.05.026. PMID 15200951.
- Nishio H, Walsh MJ (Aug 2004). "CCAAT displacement protein/cut homolog recruits G9a histone lysine methyltransferase to repress transcription". Proceedings of the National Academy of Sciences of the United States of America. 101 (31): 11257–62. doi:10.1073/pnas.0401343101. PMC 509191. PMID 15269344.
- Collins RE, Tachibana M, Tamaru H, Smith KM, Jia D, Zhang X, Selker EU, Shinkai Y, Cheng X (Feb 2005). "In vitro and in vivo analyses of a Phe/Tyr switch controlling product specificity of histone lysine methyltransferases". The Journal of Biological Chemistry. 280 (7): 5563–70. doi:10.1074/jbc.M410483200. PMC 2696276. PMID 15590646.
{{cite journal}}: CS1 maint: unflagged free DOI (link) - Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (Oct 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
- Duan Z, Zarebski A, Montoya-Durango D, Grimes HL, Horwitz M (Dec 2005). "Gfi1 coordinates epigenetic repression of p21Cip/WAF1 by recruitment of histone lysine methyltransferase G9a and histone deacetylase 1". Molecular and Cellular Biology. 25 (23): 10338–51. doi:10.1128/MCB.25.23.10338-10351.2005. PMC 1291230. PMID 16287849.
- Kimura K, Wakamatsu A, Suzuki Y, Ota T, Nishikawa T, Yamashita R, Yamamoto J, Sekine M, Tsuritani K, Wakaguri H, Ishii S, Sugiyama T, Saito K, Isono Y, Irie R, Kushida N, Yoneyama T, Otsuka R, Kanda K, Yokoi T, Kondo H, Wagatsuma M, Murakawa K, Ishida S, Ishibashi T, Takahashi-Fujii A, Tanase T, Nagai K, Kikuchi H, Nakai K, Isogai T, Sugano S (Jan 2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Research. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.
- Beausoleil SA, Villén J, Gerber SA, Rush J, Gygi SP (Oct 2006). "A probability-based approach for high-throughput protein phosphorylation analysis and site localization". Nature Biotechnology. 24 (10): 1285–92. doi:10.1038/nbt1240. PMID 16964243.
- Reeves M, Murphy J, Greaves R, Fairley J, Brehm A, Sinclair J (Oct 2006). "Autorepression of the human cytomegalovirus major immediate-early promoter/enhancer at late times of infection is mediated by the recruitment of chromatin remodeling enzymes by IE86". Journal of Virology. 80 (20): 9998–10009. doi:10.1128/JVI.01297-06. PMC 1617317. PMID 17005678.
- Estève PO, Chin HG, Smallwood A, Feehery GR, Gangisetty O, Karpf AR, Carey MF, Pradhan S (Nov 2006). "Direct interaction between DNMT1 and G9a coordinates DNA and histone methylation during replication". Genes & Development. 20 (22): 3089–103. doi:10.1101/gad.1463706. PMC 1635145. PMID 17085482.
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