Arabidopsis SWR1-associated protein methyl-CpG-binding domain 9 is required for histone H2A.Z deposition

Magdalena E. Potok, Yafei Wang, Linhao Xu, Zhenhui Zhong, Wanlu Liu, Suhua Feng, Bilguudei Naranbaatar, Shima Rayatpisheh, Zonghua Wang, James A. Wohlschlegel, Israel Ausin () and Steven E. Jacobsen ()
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Magdalena E. Potok: University of California, Los Angeles
Yafei Wang: Fujian Agriculture and Forestry University
Linhao Xu: Fujian Agriculture and Forestry University
Zhenhui Zhong: University of California, Los Angeles
Wanlu Liu: University of California, Los Angeles
Suhua Feng: University of California, Los Angeles
Bilguudei Naranbaatar: University of California, Los Angeles
Shima Rayatpisheh: University of California, Los Angeles
Zonghua Wang: Fujian Agriculture and Forestry University
James A. Wohlschlegel: University of California, Los Angeles
Israel Ausin: Fujian Agriculture and Forestry University
Steven E. Jacobsen: University of California, Los Angeles

Nature Communications, 2019, vol. 10, issue 1, 1-14

Abstract: Abstract Deposition of the histone variant H2A.Z by the SWI2/SNF2-Related 1 chromatin remodeling complex (SWR1-C) is important for gene regulation in eukaryotes, but the composition of the Arabidopsis SWR1-C has not been thoroughly characterized. Here, we aim to identify interacting partners of a conserved Arabidopsis SWR1 subunit ACTIN-RELATED PROTEIN 6 (ARP6). We isolate nine predicted components and identify additional interactors implicated in histone acetylation and chromatin biology. One of the interacting partners, methyl-CpG-binding domain 9 (MBD9), also strongly interacts with the Imitation SWItch (ISWI) chromatin remodeling complex. MBD9 is required for deposition of H2A.Z at a distinct subset of ARP6-dependent loci. MBD9 is preferentially bound to nucleosome-depleted regions at the 5’ ends of genes containing high levels of activating histone marks. These data suggest that MBD9 is a SWR1-C interacting protein required for H2A.Z deposition at a subset of actively transcribing genes.

Date: 2019
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DOI: 10.1038/s41467-019-11291-w

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