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Reference: D'Arcy S and Luger K (2011) Understanding histone acetyltransferase Rtt109 structure and function: how many chaperones does it take? Curr Opin Struct Biol 21(6):728-34

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Abstract


Rtt109 (Regulator of Ty1 Transposition 109) is a fungal-specific histone acetyltransferase required for modification of histone H3 K9, K27 and K56. These acetylations are associated with nascent histone H3 and play an integral role in replication-coupled and repair-coupled nucleosome assembly. Rtt109 is unique among acetyltransferases as it is activated by a histone chaperone; either Vps75 (Vacuolar Protein Sorting 75) or Asf1 (Anti-silencing Function 1). Recent biochemical, structural and genetic studies have shed light on the intricacies of this activation. It is now clear that Rtt109-Asf1 acetylates K56, while Rtt109-Vps75 acetylates K9 and K27. This reinforces that Asf1 and Vps75 activate Rtt109 via distinct molecular mechanisms. Structures of Rtt109-Vps75 further imply that Vps75 positions histone H3 in the Rtt109 active site. These structures however raise questions regarding the stoichiometry of the Rtt109-Vps75 complex. This has ramifications for determining the physiological Rtt109 substrate.CI - Copyright (c) 2011 Elsevier Ltd. All rights reserved.

Reference Type
Journal Article | Review | Research Support, Non-U.S. Gov't | Research Support, N.I.H., Extramural
Authors
D'Arcy S, Luger K
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