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Journal of Biochemistry Advance Access published online on March 29, 2007
Journal of Biochemistry, doi:10.1093/jb/mvm083
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© 2007 The Japanese Biochemical Society

The nuclear actin-related protein of Saccharomyces cerevisiae, Arp4, directly interacts with the histone acetyltransferase Esa1p

Ferdinand Steinboeck*, Alexandra Bogusch, Alexius Kaufmann+ and Erich Heidenreich

Institute of Cancer Research, Department of Medicine I, Medical University of Vienna, Borschkegasse 8a, A-1090 Vienna, Austria

* Corresponding author: Dr. Ferdinand Steinboeck, Medical University of Vienna, Department of Medicine I Division: Institute of Cancer Research, Borschkegasse 8a, A-1090 Vienna, Austria; Tel.: 43-1-4277 65212; FAX: 43-1-4277-9651, E-mail: ferdinand.steinboeck{at}meduniwien.ac.at

Received February 8, 2007; Accepted March 18, 2007


  Abstract

Ten actin-related proteins are known in Saccharomyces cerevisiae, classified into Arps1-10 according to their relatedness to actin. Arp4, a nuclear protein, essential for viability of S. cerevisiae, is a component of at least three chromatin-modifying complexes, one of which is the histone acetyltransferase complex NuA4. Since recent data point to a role for Arp4 in the recruitment to specific sites of interaction, we tested if Arp4 directly interacts with the histone acetyltransferase Esa1p, which is the catalytic subunit of NuA4. We observed that Arp4 directly binds to Esa1p, whereas Act1p, which is also a component of the NuA4 complex, does not interact with Esa1p. The interaction of Arp4 and Esa1p was not abolished by a deletion of one or both of the specific insertions present in the ARP4 gene. We propose that the interaction of Arp4 with Esa1p is crucial for proper functioning and targeting of the NuA4 complex.

Key Words: Arp4, Esa1, actin, histone, acetylation, NuA4

+ present address: Department of Anesthesiology and Intensive Care Medicine (B), Medical University of Vienna, Waehringer Guertel 18-20, A-1090 Vienna, Austria


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