REVIEW: Structure and Function of MYST1 Histone Acetyltransferase in the Interactome of Animal Cells

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R. I. Dmitriev^*, M. I. Shakhparonov, and N. B. Pestov

Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya 16/10, 117997 Moscow, Russia; E-mail: enisseisk@gmail.com

^* To whom correspondence should be addressed.

Received September 18, 2007; Revision received January 22, 2008

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The major function of protein MYST1 is acetylation of histone H4 at the K16 residue. This modification is essential for chromatin remodeling and is used for regulation of gene expression in eukaryotes. MYST1 is a part of multiprotein complexes that accomplish functions of male X-chromosome activation and thereby functions of dosage compensation in drosophila and, in mammals, global acetylation of histone H4 K16. Recently, novel functional links between MYST1 and proteins ATM and p53 have been observed, and it is recognized that MYST1 plays a role in tumor suppression mechanisms. In the present review, we examine novel data about functional composition and mechanisms of MYST1-containing complexes. Interplay between MYST1 and other components of the animal cell interactome is also discussed.

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KEY WORDS: hampin, MYST1, MSL, compensasome, chromatin structure rearrangement

DOI: 10.1134/S0006297908080014

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