The BioGRID | PUBLICATION VIEW

	J. Biochem. May (2007); 141(5):661-8
The nuclear actin-related protein of Saccharomyces cerevisiae, Arp4, directly interacts with the histone acetyltransferase Esa1p-
Steinboeck F, Bogusch A, Kaufmann A, Heidenreich E
Department of Medicine I, Institute of Cancer Research, Medical University of Vienna, Borschkegasse 8a, A-1090 Vienna, Austria- ferdinand-steinboeck@meduniwien-ac-at
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 -HAT- 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 HAT Esa1p that 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-
[PUBMED: 17395615]