3qb0
From Proteopedia
Crystal structure of Actin-related protein Arp4 from S. cerevisiae complexed with ATP
Structural highlights
Function[ARP4_YEAST] Chromatin interaction component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histone H4 and H2A. The NuA4 complex is also involved in DNA repair. ARP4 recognizes H2AS128ph (gamma-H2A) and is required for NuA4 complex integrity. Component of the SWR1 complex which mediates the ATP-dependent exchange of histone H2A for the H2A variant HZT1 leading to transcriptional regulation of selected genes by chromatin remodeling. Component of the INO80 complex which remodels chromatin by shifting nucleosomes. Its ability to induce transcription of some phosphate-responsive genes is modulated by inositol polyphosphates. The INO80 complex is involved in DNA repair by associating to gamma-H2A as a response to DNA damage.[1] [2] [3] [4] [5] [6] [7] [8] [9] Publication Abstract from PubMedNuclear actin and actin-related proteins (Arps) are integral components of various chromatin-remodelling complexes. Actin in such nuclear assemblies does not form filaments but associates in defined complexes, for instance with Arp4 and Arp8 in the INO80 remodeller. To understand the relationship between nuclear actin and its associated Arps and to test the possibility that Arp4 and Arp8 help maintain actin in defined states, we structurally analysed Arp4 and Arp8 from Saccharomyces cerevisiae and tested their biochemical effects on actin assembly and disassembly. The solution structures of isolated Arp4 and Arp8 indicate them to be monomeric and the crystal structure of ATP-Arp4 reveals several differences to actin that explain why Arp4 does not form filaments itself. Remarkably, Arp4, assisted by Arp8, influences actin polymerization in vitro and is able to depolymerize actin filaments. Arp4 likely forms a complex with monomeric actin via the barbed end. Our data thus help explaining how nuclear actin is held in a discrete complex within the INO80 chromatin remodeller. Structural biochemistry of nuclear actin-related proteins 4 and 8 reveals their interaction with actin.,Fenn S, Breitsprecher D, Gerhold CB, Witte G, Faix J, Hopfner KP EMBO J. 2011 Apr 15. PMID:21499228[10] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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Categories: Atcc 18824 | Breitsprecher, D | Faix, J | Fenn, S | Gerhold, C B | Hopfner, K P | Witte, G | Actin fold | Atp binding | Nucleus | Structural protein