Biochemical Analysis of Histone Deacetylase-independent Transcriptional Repression by MeCP2

Theisen, Joshua W. M.; Gucwa, James Stephen; Yusufzai, Timur; Khuong, Mai T.; Kadonaga, James T.

doi:10.1074/jbc.m112.438697

Cited by 10 publications

(8 citation statements)

References 25 publications

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“…The mechanism may contribute to the delayed repression of PP1Cβ, consistent with HDAC2 recruitment by Mecp2 in a complex silencing transcriptional activity (Nan et al, 1998;Harikrishnan et al, 2005). *p < 0.05, ***p < 0.001. mechanism of MeCP2-mediated repression has been reported to be particularly relevant in neurons that have high levels of methylated CpG and MeCP2 (Theisen et al, 2013). The effects of cocaine and food reward and that of related operant conditioning on PP1Cβ mRNA level were evaluated by quantitative RT-PCR 24 h after the beginning of the last session of cocaine (a, b) and food pellets (c, d) administration in the medial part of the PFCx and in the CPu, as indicated.…”

Section: Discussionmentioning

confidence: 99%

Differential regulation of MeCP2 and PP1 in passive or voluntary administration of cocaine or food

Bodetto

Romieu

Sartori

et al. 2014

Int. J. Neuropsychopharm.

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Cocaine exposure induces changes in the expression of numerous genes, in part through epigenetic modifications. We have initially shown that cocaine increases the expression of the chromatin remodeling protein methyl-CpG binding protein 2 (MeCP2) and characterized the protein phosphatase-1Cβ (PP1Cβ) gene, as repressed by passive i.p. cocaine injections through a Mecp2-mediated mechanism involving de novo DNA methylation. Both proteins being involved in learning and memory processes, we investigated whether voluntary cocaine administration would similarly affect their expression using an operant self-administration paradigm. Passive and voluntary i.v. cocaine intake was found to induce Mecp2 and to repress PP1Cβ in the prefrontal cortex and the caudate putamen. This observation is consistent with the role of Mecp2 acting as a transcriptional repressor of PP1Cβ and shows that passive intake was sufficient to alter their expression. Surprisingly, striking differences were observed under the same conditions in food-restricted rats tested for food pellet delivery. In the prefrontal cortex and throughout the striatum, both proteins were induced by food operant conditioning, but remained unaffected by passive food delivery. Although cocaine and food activate a common reward circuit, changes observed in the expression of other genes such as reelin and GAD67 provide new insights into molecular mechanisms differentiating neuroadaptations triggered by each reinforcer. The identification of hitherto unknown genes differentially regulated by drugs of abuse and a natural reinforcer should improve our understanding of how two rewarding stimuli differ in their ability to drive behavior.

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Section: Discussionmentioning

confidence: 99%

Differential regulation of MeCP2 and PP1 in passive or voluntary administration of cocaine or food

Bodetto

Romieu

Sartori

et al. 2014

Int. J. Neuropsychopharm.

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“…Human Nuclear Extract-HeLa nuclear extracts (HSK) were prepared as described (31) with modified Buffer HEG containing 25 mM HEPES-K ϩ (pH 7.6), 0.1 mM EDTA, 10% (v/v) glycerol, 0.01% NP40, 0.1 M KCl, 1 mM DTT, 1 mM benzamidine-HCl, 0.2 mM PMSF, 1 mM Na 2 S 2 O 5 , and 10 mM ␤-phosphoglycerol. Dignam nuclear extracts were prepared as described previously (32).…”

Section: Methodsmentioning

confidence: 99%

RNA Polymerase III Accurately Initiates Transcription from RNA Polymerase II Promoters in Vitro

Duttke

2014

Journal of Biological Chemistry

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Background: RNA polymerase II (Pol II) and III (Pol III) transcription systems are reported to regulate non-overlapping sets of genes. Results: Pol III can initiate transcription from Pol II promoters with AT-rich sequence. The DNA template to nuclear extract ratio determines the predominant polymerase. Conclusion: Pol II and Pol III transcription initiation can overlap. Significance: RNA polymerase specificity is variable and depends on the transcription conditions.

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“…In addition to studies involving gene expression, SCPs have been employed in biochemical and biophysical analyses of TFIID and the PIC (see, for example: Cianfrocco et al 2013;Louder et al 2016). There are also CpG-deficient SCPs that are resistant to repression by CpG methylation (Theisen et al 2013). For studies in Drosophila, the Drosophila synthetic core promoter (DSCP;Pfeiffer et al 2008) has been used in the analysis of enhancer activity (see, for example: Pfeiffer et al 2008;Arnold et al 2013;Zabidi et al 2015).…”

Section: Practical Applications Of Synthetic Core Promotersmentioning

confidence: 99%

The RNA Polymerase II Core Promoter in Drosophila

Ngoc¹,

Kassavetis²,

Kadonaga

2019

Genetics

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Transcription by RNA polymerase II initiates at the core promoter, which is sometimes referred to as the "gateway to transcription." Here, we describe the properties of the RNA polymerase II core promoter in Drosophila. The core promoter is at a strategic position in the expression of genes, as it is the site of convergence of the signals that lead to transcriptional activation. Importantly, core promoters are diverse in terms of their structure and function. They are composed of various combinations of sequence motifs such as the TATA box, initiator (Inr), and downstream core promoter element (DPE). Different types of core promoters are transcribed via distinct mechanisms. Moreover, some transcriptional enhancers exhibit specificity for particular types of core promoters. These findings indicate that the core promoter is a central component of the transcriptional apparatus that regulates gene expression.

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Biochemical Analysis of Histone Deacetylase-independent Transcriptional Repression by MeCP2

Cited by 10 publications

References 25 publications

Differential regulation of MeCP2 and PP1 in passive or voluntary administration of cocaine or food

Differential regulation of MeCP2 and PP1 in passive or voluntary administration of cocaine or food

RNA Polymerase III Accurately Initiates Transcription from RNA Polymerase II Promoters in Vitro

The RNA Polymerase II Core Promoter in Drosophila

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