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Readers of histone modifications.

06:14 EDT 21st May 2013 | BioPortfolio

Summary of "Readers of histone modifications."

Histone modifications not only play important roles in regulating chromatin structure and nuclear processes but also can be passed to daughter cells as epigenetic marks. Accumulating evidence suggests that the key function of histone modifications is to signal for recruitment or activity of downstream effectors. Here, we discuss the latest discovery of histone-modification readers and how the modification language is interpreted.Cell Research advance online publication 22 March 2011; doi: 10.1038/cr.2011.42.

Affiliation

Department of Molecular Biology, UT Southwestern Medical Center, Dallas, TX 75390-9148, USA;

Journal Details

This article was published in the following journal.

Name: Cell research
ISSN: 1748-7838
Pages:

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Medical and Biotech [MESH] Definitions

Histone Deacetylase 1

A histone deacetylase subtype that is found along with HISTONE DEACETYLASE 2; RETINOBLASTOMA-BINDING PROTEIN 4; and RETINOBLASTOMA-BINDING PROTEIN 7 as core components of histone deacetylase complexes.

Histone Deacetylase 2

A histone deacetylase subtype that is found along with HISTONE DEACETYLASE 1; RETINOBLASTOMA-BINDING PROTEIN 4; and RETINOBLASTOMA-BINDING PROTEIN 7 as core components of histone deacetylase complexes.

Protein Processing, Post-translational

Any of various enzymatically catalyzed post-translational modifications of PEPTIDES or PROTEINS in the cell of origin. These modifications include carboxylation; HYDROXYLATION; ACETYLATION; PHOSPHORYLATION; METHYLATION; GLYCOSYLATION; ubiquitination; oxidation; proteolysis; and crosslinking and result in changes in molecular weight and electrophoretic motility.

Sin3 Histone Deacetylase And Corepressor Complex

A multisubunit enzyme complex that regulates GENETIC TRANSCRIPTION by deacetylating the HISTONE residues of NUCLEOSOMES.

Histone Deacetylase Inhibitors

Compounds that inhibit HISTONE DEACETYLASES. This class of drugs may influence gene expression by increasing the level of acetylated HISTONES in specific CHROMATIN domains.

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