The CBP co-activator is a histone acetyltransferase

Article Abstract:

The functional activity of the transcriptional co-activator CBP protein, was investigated using immunoprecipitation-histone acetyltransferase (IP-HAT) assay. The results confirmed that the protein possesses HAT activity and that its HAT domain is adjacent to the binding site for the transcriptional activator E1A. It was also deduced from the findings that E1A, as an activator of transcription, functions via a mechanism wherein the CBP-associated HAT activity is targeted to its specific promoters.

Analysis, Usage, Transferases, Cell culture, Tissue culture, Molecular genetics, Immunoassay, Enzymatic analysis

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Retinoblastoma protein recruits histone deacetylase to repress transcription

Article Abstract:

Histone deacetylase activity is ascribed to HDAC1 and HDAC2, mammalian proteins, existing in a complex with other proteins, and are implicated in transcriptional repression due to nucleosome remodelling. Rbp48, a known Rb-binding protein, is found in the deacetylase complex, and an investigation was undertaken to determine if the Rb repressor is linked to histone deacetylase activity, and results indicated its association with deacetylase activity in vivo.

Observations, Histones, Retinoblastoma

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Selective recognition of methylated lysine 9 on histone H3 by the HP1 chromo domain

Article Abstract:

Research is presented concerning the ability of the histone H3 which has been methylated at lysine 9 to bind with the heterochromatin protein. The gene silencing activity of heterochromatin proteins in Drosophila is discussed.

Physiological aspects, Proteins, Drosophila, Letter to the Editor, Methylation

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