Histone H1 and H3 dephosphorylation are differentially regulated by radiation-induced signal transduction pathways

C. Y. Guo, C. Mizzen, Y. Wang, J. M. Larner

Research output: Contribution to journalArticlepeer-review

Abstract

We recently demonstrated that linker histone H1, which is thought to have a fundamental role in higher-order chromatin structure, becomes transiently dephosphorylated after ionizing radiation (IR) in a mutated ataxia telangiectasia (ATM) dependent manner. To establish whether H1 dephosphorylation was a component of a damage-response pathway that included dephosphorylation of other histones, we asked whether H3 was dephosphorylated in response to IR in a manner similar to H1. H1 and H3 are maximally phosphorylated in metaphase and both are dephosphorylated after IR. However, the duration of IR-induced H3 dephosphorylation is significantly longer than that of IR-induced H1 dephosphorylation. Moreover, H1 dephosphorylation is ATM-dependent, whereas H3 dephosphorylation is ATM-independent. These observations suggest that the damage-sensing pathways regulating H3 and H1 dephosphorylation diverge upstream of ATM.

Original languageEnglish (US)
Pages (from-to)5667-5672
Number of pages6
JournalCancer Research
Volume60
Issue number20
StatePublished - Oct 15 2000

ASJC Scopus subject areas

  • Oncology
  • Cancer Research

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