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Molecular and Cellular Biology, July 2002, p. 5047-5053, Vol. 22, No. 14
0270-7306/02/$04.00+0     DOI: 10.1128/MCB.22.14.5047-5053.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Yng1p Modulates the Activity of Sas3p as a Component of the Yeast NuA3 Histone Acetyltransferase Complex

LeAnn Howe,1 Thomas Kusch,1 Nemone Muster,2 Ranjana Chaterji,1 John R. Yates, III,2 and Jerry L. Workman1*

Howard Hughes Medical Institute, Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, Pennsylvania 16802-4500,1 Department of Cell Biology, The Scripps Research Institute, La Jolla, California 920372

Received 4 December 2001/ Returned for modification 15 January 2002/ Accepted 16 April 2002

The mammalian ING1 gene encodes a tumor suppressor required for the function of p53. In this study we report a novel function for YNG1, a yeast homolog of ING1. Yng1p is a stable component of the NuA3 histone acetyltransferase complex, which contains Sas3p, the yeast homolog of the mammalian MOZ proto-oncogene product, as its catalytic subunit. Yng1p is required for NuA3 function in vivo but surprisingly is not required for the integrity of the complex. Instead, we find that Yng1p mediates the interaction of Sas3p with nucleosomes and is thus required for the ability of NuA3 to modify histone tails. These data, and the observations that other ING1 homologs are found in additional yeast complexes that posttranslationally modify histones, suggest that members of the ING1 class of proteins may have broad roles in enhancing or modifying the activities of chromatin-modifying complexes, thereby regulating their activities in transcription control.

* Corresponding author. Mailing address: Howard Hughes Medical Institute, 306 Althouse Laboratory, Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA 16802. Phone: (814) 863-8256. Fax: (814) 863-0099. E-mail: jlw10{at}psu.edu.

Molecular and Cellular Biology, July 2002, p. 5047-5053, Vol. 22, No. 14
0022-538X/02/$04.00+0     DOI: 10.1128/MCB.22.14.5047-5053.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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