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. 2014 Feb;70(Pt 2):310-6.
doi: 10.1107/S1399004713027417. Epub 2014 Jan 29.

Structure of the full-length yeast Arp7-Arp9 heterodimer

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Structure of the full-length yeast Arp7-Arp9 heterodimer

Joel Lobsiger et al. Acta Crystallogr D Biol Crystallogr. 2014 Feb.

Abstract

The nuclear actin-related proteins Arp7 and Arp9 are components of the yeast SWI/SNF and RSC chromatin-remodelling complexes. The 3.1 Å 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.

Keywords: Arp; RSC; SWI/SNF; actin; chromatin remodelling; nucleus.

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