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The histone H4 acetyltransferase MOF uses a C 2 HC zinc finger for substrate recognition
Author(s) -
Akhtar Asifa,
Becker Peter B
Publication year - 2001
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1093/embo-reports/kve022
Subject(s) - zinc finger , histone , nucleosome , histone acetyltransferase , phd finger , histone acetyltransferases , acetylation , histone h4 , ring finger domain , chemistry , zinc , substrate (aquarium) , biology , genetics , microbiology and biotechnology , biochemistry , dna , gene , ecology , organic chemistry , transcription factor
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 C 2 HC‐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 C 2 HC‐type finger in nucleosome binding and HAT activity.