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Series GSE12212 Query DataSets for GSE12212
Status Public on Oct 03, 2008
Title Histone H2A.Z and DNA methylation are mutually antagonistic chromatin marks
Organism Arabidopsis thaliana
Experiment type Methylation profiling by genome tiling array
Summary Eukaryotic chromatin is separated into functional domains differentiated by posttranslational histone modifications, histone variants, and DNA methylation. Methylation is associated with repression of transcriptional initiation in plants and animals, and is frequently found in transposable elements. Proper methylation patterns are critical for eukaryotic development, and aberrant methylation-induced silencing of tumor suppressor genes is a common feature of human cancer. In contrast to methylation, the histone variant H2A.Z is preferentially deposited by the Swr1 ATPase complex near 5' ends of genes where it promotes transcriptional competence. How DNA methylation and H2A.Z influence transcription remains largely unknown. Here we show that in the plant Arabidopsis thaliana, regions of DNA methylation are quantitatively deficient in H2A.Z. Exclusion of H2A.Z is seen at sites of DNA methylation in the bodies of actively transcribed genes and in methylated transposons. Mutation of the MET1 DNA methyltransferase, which causes both losses and gains of DNA methylation, engenders opposite changes in H2A.Z deposition, while mutation of the PIE1 subunit of the Swr1 complex that deposits H2A.Z17 leads to genome-wide hypermethylation. Our findings indicate that DNA methylation can influence chromatin structure and effect gene silencing by excluding H2A.Z, and that H2A.Z protects genes from DNA methylation.

Keywords: Affinity-purification on microarray
 
Overall design All experiments were done using two channels per chip. DNA methylation experiments compared immunoprecipitated, methylated DNA to control genomic DNA. H2A.Z experiments compared whole micrococcal nuclease-treated affinity-purified chromatin to input chromatin used for affinity purification. Affinity purification was performed using either biotin-tagged H2A.Z, pulled down using streptavidin, or endogenous H2A.Z pulled down using an anti-H2A.Z antibody.
 
Contributor(s) Daniel Z, Steven H
Citation(s) 18815594
Submission date Jul 23, 2008
Last update date Mar 20, 2012
Contact name Jorja Henikoff
E-mail(s) jorja@fhcrc.org
Phone 206-667-4850
Organization name Fred Hutchinson Cancer Research Center
Department Basic Sciences
Lab Henikoff
Street address 1100 Fairview AV N, A1-162
City Seattle
State/province WA
ZIP/Postal code 98109-1024
Country USA
 
Platforms (1)
GPL3371 FHCRC Arabidopsis Tiling Array
Samples (21)
GSM307373 Zilberman H2A.Z IP/total DNA 90984 (BLRP-1)
GSM307374 Zilberman H2A.Z IP/total DNA 1364702 (BLRP-2)
GSM307375 Zilberman H2A.Z IP/total DNA 1364902 (BLRP-3)
Relations
BioProject PRJNA113725

Download family Format
SOFT formatted family file(s) SOFTHelp
MINiML formatted family file(s) MINiMLHelp
Series Matrix File(s) TXTHelp

Supplementary file Size Download File type/resource
GSE12212_RAW.tar 347.0 Mb (http)(custom) TAR (of GFF, PAIR)
Processed data included within Sample table

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