Article

 

Heterochromatin Controls γH2A Localization in Neurospora crassa Public Deposited

Downloadable Content

Download PDF
https://ir.library.oregonstate.edu/concern/articles/rr1722844

Descriptions

Attribute NameValues
Creator
Abstract
  • In response to genotoxic stress, ATR and ATM kinases phosphorylate H2A in fungi and H2AX in animals on a C-terminal serine. The resulting modified histone, called γH2A, recruits chromatin-binding proteins that stabilize stalled replication forks or promote DNA double-strand-break repair. To identify genomic loci that might be prone to replication fork stalling or DNA breakage in Neurospora crassa, we performed chromatin immunoprecipitation (ChIP) of γH2A followed by next-generation sequencing (ChIP-seq). γH2A-containing nucleosomes are enriched in Neurospora heterochromatin domains. These domains are comprised of A·T-rich repetitive DNA sequences associated with histone H3 methylated at lysine-9 (H3K9me), the H3K9me-binding protein heterochromatin protein 1 (HP1), and DNA cytosine methylation. H3K9 methylation, catalyzed by DIM-5, is required for normal γH2A localization. In contrast, γH2A is not required for H3K9 methylation or DNA methylation. Normal γH2A localization also depends on HP1 and a histone deacetylase, HDA-1, but is independent of the DNA methyltransferase DIM-2. γH2A is globally induced in dim-5 mutants under normal growth conditions, suggesting that the DNA damage response is activated in these mutants in the absence of exogenous DNA damage. Together, these data suggest that heterochromatin formation is essential for normal DNA replication or repair.
Resource Type
DOI
Date Available
Date Issued
Citation
  • Sasaki, T., Lynch, K. L., Mueller, C. V., Friedman, S., Freitag, M., & Lewis, Z. A. (2014). Heterochromatin controls γH2A localization in Neurospora crassa. Eukaryotic Cell, 13(8), 990-1000. doi:10.1128/EC.00117-14
Journal Title
Journal Volume
  • 13
Journal Issue/Number
  • 8
Rights Statement
Funding Statement (additional comments about funding)
  • This work was funded in part by a grant to Z.A.L. from the March ofDimes Foundation (grant 5-FY14-89) and by a grant to M.F. from theNational Institutes of Health (grant GM097637).
Publisher
Peer Reviewed
Language
Replaces

Relationships

Parents:

This work has no parents.

Items