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ICBP90, a novel methyl K9 H3 binding protein linking protein ubiquitination with heterochromatin formation

Panagiota Karagianni1, Larbi Amazit, Jun Qin

  • 1Department of Medicine, Harvard Medical School and Massachusetts General Hospital Cancer Center, Building 149, Room 7-213, 13th Street, Charlestown, MA 02129, USA. pkaragianni@partners.org

Molecular and Cellular Biology
|October 31, 2007
PubMed

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Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

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Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

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These groups modify specific amino acids in a protein.
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Chromatin Immunoprecipitation- ChIP

Chromatin immunoprecipitation, or ChIP, is an antibody-based technique used to identify sites on DNA that bind to transcription factors of interest or histone proteins. It also helps determine the type of histone modifications such as acetylation, phosphorylation, or methylation.
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Immunoprecipitation

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Chromatin Immunoprecipitation
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Spreading of Chromatin Modifications

The histone proteins in the nucleosomes are post-translationally modified (PTM) to increase or decrease access to DNA. The commonly observed PTMs are methylation, acetylation, phosphorylation, and ubiquitination of lysine amino acids in the histone H3 tail region. These histone modifications have specific meaning for the cell. Hence, they are called "histone code". The protein complex involved in histone modification is termed as "reader-writer" complex.
Writers
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