Histone H1 phosphorylation is associated with transcription by RNA polymerases I and II

Yupeng Zheng, Sam John, James J. Pesavento, Jennifer R. Schultz-Norton, R. Louis Schiltz, Sonjoon Baek, Ann M. Nardulli, Gordon L. Hager, Neil L. Kelleher, Craig A. Mizzen

Research output: Contribution to journalArticlepeer-review

Abstract

Histone H1 phosphorylation affects chromatin condensation and function, but little is known about how specific phosphorylations impact the function of H1 variants in higher eukaryotes. In this study, we show that specific sites in H1.2 and H1.4 of human cells are phosphorylated only during mitosis or during both mitosis and interphase. Antisera generated to individual H1.2/H1.4 interphase phosphorylations reveal that they are distributed throughout nuclei and enriched in nucleoli. Moreover, interphase phosphorylated H1.4 is enriched at active 45S preribosomal RNA gene promoters and is rapidly induced at steroid hormone response elements by hormone treatment. Our results imply that site-specific interphase H1 phosphorylation facilitates transcription by RNA polymerases I and II and has an unanticipated function in ribosome biogenesis and control of cell growth. Differences in the numbers, structure, and locations of interphase phosphorylation sites may contribute to the functional diversity of H1 variants.

Original languageEnglish (US)
Pages (from-to)407-415
Number of pages9
JournalJournal of Cell Biology
Volume189
Issue number3
DOIs
StatePublished - May 3 2010

ASJC Scopus subject areas

  • Cell Biology

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