Structure of Actin-related protein 8 and its contribution to nucleosome binding
By C. Gerhold, Duane D. Winkler, K. Lakomek, F. U. Seifert, S. Fenn, B. Kessler, Gregor Witte, K. Luger, K. Hopfner. 2012
56 citations recorded by the source corpus.
Nuclear actin-related proteins (Arps) are subunits of several chromatin remodelers, but their molecular functions within these complexes are unclear. We report the crystal structure of the INO80 complex subunit Arp8 in its ATP-bound form. Human Arp8 has several insertions in the conserved actin fold that explain its inability to polymerize. Most remarkably, one insertion wraps over the active site cleft and appears to rigidify the domain architecture, while active site features shared with actin suggest an allosterically controlled ATPase activity. Quantitative binding studies with nucleosomes and histone complexes reveal that Arp8 and the Arp8–Arp4–actin-HSA sub-complex of INO80 strongly prefer nucleosomes and H3–H4 tetramers over H2A–H2B dimers, suggesting that Arp8 functions as a nucleosome recognition module. In contrast, Arp4 prefers free (H3–H4)2 over nucleosomes and may serve remodelers through binding to (dis)assembly intermediates in the remodeling reaction.
Subfields: Molecular Biology
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In Molecular Biology
- Kuldip K. Paliwal
- Jack Hanson
- Yaoqi Zhou
- Thomas Litfin
- Yuedong Yang
- Jinbo Xu
- Sheng Wang
- Jianlin Cheng
Citations in the corpus
- SPOT-Disorder2: Improved Protein Intrinsic Disorder Prediction by Ensembled Deep Learning (2019, background): “Despite being labeled as ordered by DisProt, there is no experimental evidence to support this labeling as these residues are missing from the solved X-ray structure [45,53].”