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Molecular and Cellular Biology, November 2006, p. 7871-7879, Vol. 26, No. 21
0270-7306/06/$08.00+0     doi:10.1128/MCB.00573-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

The Yng1p Plant Homeodomain Finger Is a Methyl-Histone Binding Module That Recognizes Lysine 4-Methylated Histone H3{triangledown}

David G. E. Martin,1 Kristin Baetz,2,{dagger} Xiaobing Shi,3 Kay L. Walter,3 Vicki E. MacDonald,1 Martin J. Wlodarski,1 Or Gozani,3 Philip Hieter,2 and LeAnn Howe1*

Department of Biochemistry and Molecular Biology,1 Michael Smith Laboratories, University of British Columbia, Vancouver, British Columbia, Canada,2 Department of Biological Sciences, Stanford University, Stanford, California3

Received 1 April 2006/ Returned for modification 2 June 2006/ Accepted 1 August 2006

The ING (inhibitor of growth) protein family includes a group of homologous nuclear proteins that share a highly conserved plant homeodomain (PHD) finger domain at their carboxyl termini. Members of this family are found in multiprotein complexes that posttranslationally modify histones, suggesting that these proteins serve a general role in permitting various enzymatic activities to interact with nucleosomes. There are three members of the ING family in Saccharomyces cerevisiae: Yng1p, Yng2p, and Pho23p. Yng1p is a component of the NuA3 histone acetyltransferase complex and is required for the interaction of NuA3 with chromatin. To gain insight into the function of the ING proteins, we made use of a genetic strategy to identify genes required for the binding of Yng1p to histones. Using the toxicity of YNG1 overexpression as a tool, we showed that Yng1p interacts with the amino-terminal tail of histone H3 and that this interaction can be disrupted by loss of lysine 4 methylation within this tail. Additionally, we mapped the region of Yng1p required for overexpression of toxicity to the PHD finger, showed that this region capable of binding lysine 4-methylated histone H3 in vitro, and demonstrated that mutations of the PHD finger that abolish binding in vitro are no longer toxic in vivo. These results identify a novel function for the Yng1p PHD finger in promoting stabilization of the NuA3 complex at chromatin through recognition of histone H3 lysine 4 methylation.

* Corresponding author. Mailing address: Department of Biochemistry and Molecular Biology, University of British Columbia, 2350 Health Sciences Mall, Vancouver, British Columbia V6T 1Z3, Canada. Phone: (604) 822-6297. Fax: (604) 822-5227. E-mail: ljhowe{at}interchange.ubc.ca.

{triangledown} Published ahead of print on 21 August 2006.

{dagger} Present address: Ottawa Institute of Systems Biology, Department of Biochemistry, Microbiology, and Immunology, University of Ottawa, Ottawa, Ontario, Canada.

Molecular and Cellular Biology, November 2006, p. 7871-7879, Vol. 26, No. 21
0270-7306/06/$08.00+0     doi:10.1128/MCB.00573-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



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