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

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 o...

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Published in:The Journal of cell biology 2010-05, Vol.189 (3), p.407-415
Main Authors: Zheng, Yupeng, John, Sam, Pesavento, James J, Schultz-Norton, Jennifer R, Schiltz, R. Louis, Baek, Sonjoon, Nardulli, Ann M, Hager, Gordon L, Kelleher, Neil L, Mizzen, Craig A
Format: Article
Language:English
Subjects:
Antibodies
Biochemistry
Cell Line
Cell nucleolus
Cell Nucleus - metabolism
Chromatin
DNA, Ribosomal - metabolism
Eukaryotes
G2 Phase
HeLa Cells
Histones
Histones - metabolism
Humans
Interphase
Microscopy, Fluorescence
Mitosis
Phosphorylation
Promoter Regions, Genetic
Proteins
Ribonucleic acid
Ribosomal DNA
RNA
RNA polymerase
RNA Polymerase I - metabolism
RNA Polymerase II - metabolism
Transcription, Genetic
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Summary: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.
ISSN:0021-9525
1540-8140
DOI:10.1083/jcb.201001148