3wee | pdb_00003wee
Structure of the full-length yeast Arp7-Arp9 Heterodimer
Structural highlights
FunctionARP9_YEAST Component of the chromatin structure remodeling complex (RSC), which is involved in transcription regulation and nucleosome positioning. RSC is responsible for the transfer of a histone octamer from a nucleosome core particle to naked DNA. The reaction requires ATP and involves an activated RSC-nucleosome intermediate. Remodeling reaction also involves DNA translocation, DNA twist and conformational change. As a reconfigurer of centromeric and flanking nucleosomes, RSC complex is required both for proper kinetochore function in chromosome segregation and, via a PKC1-dependent signaling pathway, for organization of the cellular cytoskeleton. This subunit is involved in transcriptional regulation. Heterodimer of ARP9 and ARP7 functions with HMG box proteins to facilitate proper chromatin architecture. Heterodimer formation is necessary for assembly into RSC complex. Part of the SWI/SNF complex, an ATP-dependent chromatin remodeling complex, is required for the positive and negative regulation of gene expression of a large number of genes. It changes chromatin structure by altering DNA-histone contacts within a nucleosome, leading eventually to a change in nucleosome position, thus facilitating or repressing binding of gene-specific transcription factors.[1] [2] [3] [4] [5] [6] [7] [8] Publication Abstract from PubMedThe nuclear actin-related proteins Arp7 and Arp9 are components of the yeast SWI/SNF and RSC chromatin-remodelling complexes. The 3.1 A resolution crystal structure reported here shows that the full-length Arp7 and Arp9 proteins exist as a dimer without a requirement for additional polypeptides. Of the 11 actin-related proteins, Arp7 and Arp9 are the only two directly demonstrated to form a dimer within this family. The Arp7-Arp9 heterodimer is unlikely to form an actin-like filament based on modelling using the structure. The Arp7-Arp9 structure reveals that its dimerization interface is not altered when bound in a complex with the SWI/SNF Snf2 HSA domain and the regulatory protein Rtt102. Structure of the full-length yeast Arp7-Arp9 heterodimer.,Lobsiger J, Hunziker Y, Richmond TJ Acta Crystallogr D Biol Crystallogr. 2014 Feb;70(Pt 2):310-6. doi:, 10.1107/S1399004713027417. Epub 2014 Jan 29. PMID:24531465[9] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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