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Cited by 632

The DOI matches its Crossref record; 25 of the 25 references it cites were found in a registry or an index.

The histone H4 acetyltransferase MOF uses a C 2 HC zinc finger for substrate recognition

Open access
Akhtar, Asifa, Becker, Peter B·2001·EMBO reports

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 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.

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Crossref · 10.1093/embo-reports/kve022

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Metadata

Authors
Akhtar, A., & Becker, P. B.
Venue
EMBO reports
Published
2001-02
Volume
2
Issue
2
Pages
113-118
ISSN
  • 1469-221X (ISSN-L)
  • 1469-3178
OpenAlex
W1988754209
Cited by
632
References
25
FWCI
9.45
Type
journal article
Language
en
Open access
bronze

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CoChat. (2026). Citation check: The histone H4 acetyltransferase MOF uses a C 2 HC zinc finger for substrate recognition. https://app.cochat.ai/papers/10.1093/embo-reports/kve022
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Akhtar, A., & Becker, P. B. (2001). The histone H4 acetyltransferase MOF uses a C 2 HC zinc finger for substrate recognition. EMBO reports. https://doi.org/10.1093/embo-reports/kve022

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.