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MOF, an Acetyl Transferase Involved in Dosage Compensation in Drosophila, Uses a CCHC Finger for Substrate Recognition

This chapter appears in the following book:

Zinc Finger Proteins: From Atomic Contact to Cellular Function

Edited by: Shiro Iuchi and Natalie Kuldell
ISBN: 0-306-48229-0
» Get more information about this book at landesbioscience.com «

Chapter authors:
Asifa Akhtar and Peter B. Becker


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The histone acetyltransferase MOF is central to the process of dosage compensation complex in Drosophila, which assures that the transcriptional activity of large parts of the male X chromosome is enhanced by about two-fold. Inactivation of the acetyl transferase activity of MOF is lethal to affected male flies. MOF belongs to the MYST family of acetylases that are involved in a wide variety of cellular processes. One characteristic structural feature of this family is the presence of a CCHC zinc finger adjacent to their acetyl-CoA binding motif. Structure-function analyses of several family members suggest that this region is important for enzymatic activity. Our detailed characterization of MOF shows that the CCHC-type zinc finger is required for interaction with the histone substrate and hence catalytic activity.

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ABBREVIATIONS

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Abbreviations for the book Zinc Finger Proteins: from Atomic Contact to Cellular Function

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