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

2019 ◽  
Author(s):  
Magdalena E. Potok ◽  
Yafei Wang ◽  
Linhao Xu ◽  
Zhenhui Zhong ◽  
Wanlu Liu ◽  
...  
Keyword(s):  
Gene Regulation ◽  
Histone Acetylation ◽  
Chromatin Remodeling ◽  
Binding Domain ◽  
The Novel ◽  
Related Protein ◽  
Interacting Protein ◽  
Chromatin Remodeling Complex ◽  
Distinct Subset ◽  
Chromatin Biology

AbstractDeposition 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 identify interacting partners of a conserved Arabidopsis SWR1 subunit, ACTIN-RELATED PROTEIN 6 (ARP6). We isolated nine predicted components, and identified additional interactors implicated in histone acetylation and chromatin biology. One of the novel interacting partners, methyl-CpG-binding domain 9 (MBD9), also strongly interacted with the Imitation SWItch (ISWI) chromatin remodeling complex. MBD9 was required for deposition of H2A.Z at a distinct subset of ARP6-dependent loci. MBD9 was 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.

scholarly journals Methyl-CpG-binding domain 9 (MBD9) is required for H2A.Z incorporation into chromatin at a subset of H2A.Z-enriched regions in the Arabidopsis genome

2018 ◽  
Author(s):  
Paja Sijacic ◽  
Dylan H. Holder ◽  
Marko Bajic ◽  
Roger B. Deal
Keyword(s):  
Arabidopsis Thaliana ◽  
Chromatin Remodeling ◽  
Potential Role ◽  
Affinity Purification ◽  
Binding Domain ◽  
Tandem Affinity Purification ◽  
Related Protein ◽  
Single Mutant ◽  
Chromatin Remodeling Complex ◽  
Associated Proteins

ABSTRACTThe SWR1 chromatin remodeling complex, which deposits the histone variant H2A.Z into nucleosomes, has been characterized in yeast and animals but had not been purified from plants. We used the conserved SWR1 subunit ACTIN RELATED PROTEIN 6 (ARP6) as bait in tandem affinity purification experiments to isolate associated proteins from Arabidopsis thaliana. We identified all 11 subunits found in yeast SWR1 and the homologous mammalian SRCAP complexes, demonstrating that this complex is conserved in plants. We also identified several additional proteins not previously associated with SWR1, including Methyl-CpG-BINDING DOMAIN 9 (MBD9). Since mbd9 mutant plants were phenotypically similar to arp6 mutants, we further explored a potential role for MBD9 in H2A.Z deposition. We found that MBD9 is required for proper H2A.Z incorporation at thousands of discrete sites, which represent a subset of the regions normally enriched with H2A.Z. Genetic analyses showed that arp6;mbd9 double mutants have far more severe phenotypes than either single mutant. In conjunction with the finding that MBD9 does not appear to be a core subunit of the Arabidopsis SWR1 complex, this suggests that MBD9 also has important roles beyond H2A.Z deposition. Our data establish the SWR1 complex as being conserved across eukaryotes and also provide new insights into the mechanisms that target H2A.Z to chromatin.

The trithorax group gene osa encodes an ARID-domain protein that genetically interacts with the brahma chromatin-remodeling factor to regulate transcription

Development ◽  
1999 ◽  
Vol 126 (4) ◽  
pp. 733-742 ◽  
Author(s):  
M. Vazquez ◽  
L. Moore ◽  
J.A. Kennison
Keyword(s):  
Gene Regulation ◽  
Chromatin Remodeling ◽  
Homeotic Gene ◽  
Dna Binding Domain ◽  
Atpase Subunit ◽  
Trithorax Group ◽  
Chromatin Remodeling Complex ◽  
P2 Promoter ◽  
Domain Protein ◽  
Arid Domain

The trithorax group gene brahma (brm) encodes the ATPase subunit of a chromatin-remodeling complex involved in homeotic gene regulation. We report here that brm interacts with another trithorax group gene, osa, to regulate the expression of the Antennapedia P2 promoter. Regulation of Antennapedia by BRM and OSA proteins requires sequences 5′ to the P2 promoter. Loss of maternal osa function causes severe segmentation defects, indicating that the function of osa is not limited to homeotic gene regulation. The OSA protein contains an ARID domain, a DNA-binding domain also present in the yeast SWI1 and Drosophila DRI proteins. We propose that the OSA protein may target the BRM complex to Antennapedia and other regulated genes.

scholarly journals Cutting Edge: A Novel, Human-Specific Interacting Protein Couples FOXP3 to a Chromatin-Remodeling Complex That Contains KAP1/TRIM28

2013 ◽  
Vol 190 (9) ◽  
pp. 4470-4473 ◽  
Author(s):  
Chunjian Huang ◽  
Sunil Martin ◽  
Christian Pfleger ◽  
Jianguang Du ◽  
Jane H. Buckner ◽  
...  
Keyword(s):  
Chromatin Remodeling ◽  
Cutting Edge ◽  
Interacting Protein ◽  
Chromatin Remodeling Complex ◽  
Human Specific

scholarly journals Histone acetylation recruits the SWR1 complex to regulate active DNA demethylation in Arabidopsis

2019 ◽  
Vol 116 (33) ◽  
pp. 16641-16650 ◽  
Author(s):  
Wen-Feng Nie ◽  
Mingguang Lei ◽  
Mingxuan Zhang ◽  
Kai Tang ◽  
Huan Huang ◽  
...  
Keyword(s):  
Dna Methylation ◽  
Conceptual Framework ◽  
Histone Acetylation ◽  
Chromatin Remodeling ◽  
Nuclear Protein ◽  
Dna Demethylation ◽  
Specific Target ◽  
Active Dna Demethylation ◽  
Chromatin Remodeling Complex ◽  
Genomic Regions

Active DNA demethylation is critical for controlling the DNA methylomes in plants and mammals. However, little is known about how DNA demethylases are recruited to target loci, and the involvement of chromatin marks in this process. Here, we identify 2 components of the SWR1 chromatin-remodeling complex, PIE1 and ARP6, as required for ROS1-mediated DNA demethylation, and discover 2 SWR1-associated bromodomain-containing proteins, AtMBD9 and nuclear protein X1 (NPX1). AtMBD9 and NPX1 recognize histone acetylation marks established by increased DNA methylation 1 (IDM1), a known regulator of DNA demethylation, redundantly facilitating H2A.Z deposition at IDM1 target loci. We show that at some genomic regions, H2A.Z and DNA methylation marks coexist, and H2A.Z physically interacts with ROS1 to regulate DNA demethylation and antisilencing. Our results unveil a mechanism through which DNA demethylases can be recruited to specific target loci exhibiting particular histone marks, providing a conceptual framework to understand how chromatin marks regulate DNA demethylation.

scholarly journals Regulation of muscle development by DPF3, a novel histone acetylation and methylation reader of the BAF chromatin remodeling complex

2008 ◽  
Vol 22 (17) ◽  
pp. 2370-2384 ◽  
Author(s):  
M. Lange ◽  
B. Kaynak ◽  
U. B. Forster ◽  
M. Tonjes ◽  
J. J. Fischer ◽  
...  
Keyword(s):  
Histone Acetylation ◽  
Chromatin Remodeling ◽  
Muscle Development ◽  
Chromatin Remodeling Complex

scholarly journals Human INO80/YY1 chromatin remodeling complex transcriptionally regulates the BRCA2- and CDKN1A-interacting protein (BCCIP) in cells

2016 ◽  
Vol 7 (10) ◽  
pp. 749-760 ◽  
Author(s):  
Jiaming Su ◽  
Yi Sui ◽  
Jian Ding ◽  
Fuqiang Li ◽  
Shuang Shen ◽  
...  
Keyword(s):  
Chromatin Remodeling ◽  
Interacting Protein ◽  
Chromatin Remodeling Complex ◽  
In Cells

scholarly journals SWI/SNF Displaces SAGA-Acetylated Nucleosomes

2006 ◽  
Vol 5 (10) ◽  
pp. 1738-1747 ◽  
Author(s):  
Mark Chandy ◽  
José L. Gutiérrez ◽  
Philippe Prochasson ◽  
Jerry L. Workman
Keyword(s):  
Transcription Factors ◽  
Rna Polymerase ◽  
Histone Acetylation ◽  
Chromatin Remodeling ◽  
Binding Sites ◽  
Saga Complex ◽  
Chromatin Remodeling Complex ◽  
Nucleosome Array ◽  
Transcription Activators

ABSTRACT SWI/SNF is a well-characterized chromatin remodeling complex that remodels chromatin by sliding nucleosomes in cis and/or displacing nucleosomes in trans. The latter mechanism has the potential to remove promoter nucleosomes, allowing access to transcription factors and RNA polymerase. In vivo, histone acetylation often precedes apparent nucleosome loss; therefore, we sought to determine whether nucleosomes containing acetylated histones could be displaced by the SWI/SNF chromatin remodeling complex. We found that SAGA-acetylated histones were lost from an immobilized nucleosome array when treated with the SWI/SNF complex. When the nucleosome array was acetylated by SAGA in the presence of bound transcription activators, it generated a peak of acetylation surrounding the activator binding sites. Subsequent SWI/SNF treatment suppressed this acetylation peak. Immunoblots indicated that SWI/SNF preferentially displaced acetylated histones from the array relative to total histones. Moreover, the Swi2/Snf2 bromodomain, an acetyl-lysine binding domain, played a role in the displacement of acetylated histones. These data indicate that targeted histone acetylation by the SAGA complex predisposes promoter nucleosomes for displacement by the SWI/SNF complex.

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