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Published online
doi:10.1083/jcb.200806072
The Journal of Cell Biology, Vol. 184, No. 2, 205-213
The Rockefeller University Press, 0021-9525 $30.00
© Wang et al.
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Histone hypercitrullination mediates chromatin decondensation and neutrophil extracellular trap formation



Yanming Wang1, Ming Li1, Sonja Stadler2,3, Sarah Correll4, Pingxin Li1, Danchen Wang1, Ryo Hayama2, Lauriebeth Leonelli2, Hyunsil Han5,6, Sergei A. Grigoryev4, C. David Allis3, and Scott A. Coonrod2

1 Center for Gene Regulation, Department of Biochemistry and Molecular Biology, Pennsylvania State University, University Park, PA 16802
2 Baker Institute for Animal Health, College of Veterinary Medicine, Cornell University, Ithaca, NY 14853
3 Laboratory of Chromatin Biology, The Rockefeller University, New York, NY 10065
4 Department of Biochemistry and Molecular Biology, Pennsylvania State University College of Medicine, Hershey, PA 17033
5 Department of Microbiology and 6 Department of Immunology, Weill Medical College of Cornell University, New York, NY 10021

Correspondence to Yanming Wang: yuw12{at}psu.edu; or Scott A. Coonrod: sac269{at}cornell.edu

Peripheral blood neutrophils form highly decondensed chromatin structures, termed neutrophil extracellular traps (NETs), that have been implicated in innate immune response to bacterial infection. Neutrophils express high levels of peptidylarginine deiminase 4 (PAD4), which catalyzes histone citrullination. However, whether PAD4 or histone citrullination plays a role in chromatin structure in neutrophils is unclear. In this study, we show that the hypercitrullination of histones by PAD4 mediates chromatin decondensation. Histone hypercitrullination is detected on highly decondensed chromatin in HL-60 granulocytes and blood neutrophils. The inhibition of PAD4 decreases histone hypercitrullination and the formation of NET-like structures, whereas PAD4 treatment of HL-60 cells facilitates these processes. The loss of heterochromatin and multilobular nuclear structures is detected in HL-60 granulocytes after PAD4 activation. Importantly, citrullination of biochemically defined avian nucleosome arrays inhibits their compaction by the linker histone H5 to form higher order chromatin structures. Together, these results suggest that histone hypercitrullination has important functions in chromatin decondensation in granulocytes/neutrophils.

Abbreviations used in this paper: Cit, citrulline; MNase, micrococcal nuclease; NET, neutrophil extracellular trap; PAD, peptidylarginine deiminase.

© 2009 Wang et al.
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