The histone H4 acetyltransferase MOF uses a C2HC zinc finger for substrate recognition.
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.
Adolf Butenandt-Institut, Molekularbiologie, Ludwig-Maximilians-Universität, München, Germany.
A
A
Akhtar
P B
PB
Becker
D000107:Acetylation; D000123:Acetyltransferases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D020134:Catalytic Domain; D029721:Drosophila Proteins; D004331:Drosophila melanogaster / Q000201:enzymology* / Q000235:genetics; D051548:Histone Acetyltransferases; D006657:Histones / Q000737:chemistry / Q000378:metabolism*; D008297:Male; D008969:Molecular Sequence Data; D009687:Nuclear Proteins; D009707:Nucleosomes / Q000737:chemistry / Q000378:metabolism*; D017354:Point Mutation / Q000235:genetics; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment; D013379:Substrate Specificity; D014960:X Chromosome / Q000235:genetics; D014982:Xenopus laevis; D016335:Zinc Fingers / Q000235:genetics
D029721:Drosophila Proteins; D006657:Histones; D009687:Nuclear Proteins; D009707:Nucleosomes; D000123:Acetyltransferases; D051548:Histone Acetyltransferases; C111063:mof protein, Drosophila