Authors
Takahito Yamasaki, Takehide Murata, Chunyuan Jin, Kohsuke Kato, Michiya Noguchi, Koji Nakade, Jianzhi Pan, Kyousuke Nagata, and Kazunari Yokoyama
Summary
Chromatin is a dynamic structure that can adopt markedly different conformations. During transcription, different conformations of chromatin act as important regulatory switches. A novel type of cellular complex, designated INHAT (inhibitor of histone acetyltransferases), was isolated recently and was shown to inhibit the HAT activity of p300/CBP and PCAF by binding to histones, preventing them from serving as substrates for acetyltransferases. This complex was demonstrated, initially, to have nucleosome-assembly activity. In order to examine whether other factors might have both HAT-inhibitory and nucleosome-assembly activities, similar to those of INHATs, we developed methods for measuring the inhibition of HAT activity and nucleosome-assembly activity in vitro and in vivo. Our methodology is particularly useful for measuring the histone-chaperone activity of specific proteins.Further details
The protocol was published on Protocol Exchange in 2007. To see the entire protocol, click on the source link.Advertisement
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