Crosstalk between histone modifications indicates that inhibition of arginine methyltransferase CARM1 activity reverses HIV latency

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Crosstalk between histone modifications indicates that inhibition of arginine methyltransferase CARM1 activity reverses HIV latency

In eukaryotic cells, the gene expression status is strictly controlled by epigenetic modifications on chromatin. The repressive status of chromatin largely contributes to HIV latency. Studies have shown that modification of histone H3K27 acts as a key molecular switch for activation or suppression of many cellular genes. In this study, we found that K27-acetylated histone H3 specifically recrui...

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Crosstalk between CARM1 Methylation and CBP Acetylation on Histone H3

BACKGROUND Dynamic changes in the modification pattern of histones, such as acetylation, phosphorylation, methylation, and ubiquitination, are thought to provide a code for the correct regulation of gene expression mostly by affecting chromatin structure and interactions of non-histone regulatory factors with chromatin. Recent studies have suggested the existence of an interplay between histone...

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Crosstalk among Histone Modifications

Histone modifications play a complex role in the regulation of transcription. Recent studies (Duncan et al., 2008; Lee et al., 2007; Li et al., 2008) reveal that regulation of histone modifications can be functionally linked to reinforce the activation or repression of gene expression.

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Phosphorylation-mediated inactivation of coactivator-associated arginine methyltransferase 1.

Multiple protein arginine methyltransferases are involved in transcriptional activation of nuclear receptors. Coactivator-associated arginine methyltransferase 1 (CARM1)-mediated histone methylation has been shown to activate nuclear receptor-dependent transcription; however, little is known about the regulation of its enzymatic activity. Here, we report that the methyltransferase activity of C...

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Small molecule inhibitors that discriminate between protein arginine N-methyltransferases PRMT1 and CARM1.

Protein arginine N-methyltransferases (PRMTs) selectively replace N-H for N-CH(3) at substrate protein guanidines, a post-translational modification important for a range of biological processes, such as epigenetic regulation, signal transduction and cancer progression. Selective chemical probes are required to establish the dynamic function of individual PRMTs. Herein, model inhibitors designe...

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ژورنال

عنوان ژورنال: Nucleic Acids Research

سال: 2017

ISSN: 0305-1048,1362-4962

DOI: 10.1093/nar/gkx550