Click here to close Hello! We notice that you are using Internet Explorer, which is not supported by Xenbase and may cause the site to display incorrectly. We suggest using a current version of Chrome, FireFox, or Safari.
XB-ART-9373
EMBO Rep 2001 Feb 01;22:113-8. doi: 10.1093/embo-reports/kve022.
Show Gene links Show Anatomy links

The histone H4 acetyltransferase MOF uses a C2HC zinc finger for substrate recognition.

Akhtar A , Becker PB .


Abstract
Site-specific acetylation of histone H4 by MOF is central to establishing the hyperactive male X chromosome in Drosophila. MOF belongs to the MYST family of histone acetyltransferases (HATs) characterized by an unusual C2HC-type zinc finger close to their HAT domains. The function of these rare zinc fingers is unknown. We found that this domain is essential for HAT activity, in addition to the established catalytic domain. MOF uses its zinc finger to contact the globular part of the nucleosome as well as the histone H4 N-terminal tail substrate. Point mutations that leave the zinc-finger structure intact nevertheless abolish its interaction with the nucleosome. Our data document a novel role of the C2HC-type finger in nucleosome binding and HAT activity.

PubMed ID: 11258702
PMC ID: PMC1083818
Article link: EMBO Rep


Species referenced: Xenopus laevis
Genes referenced: h4c4 kat8

References [+] :
Akhtar, Activation of transcription through histone H4 acetylation by MOF, an acetyltransferase essential for dosage compensation in Drosophila. 2000, Pubmed