Journal article

Publication year: 2005

Pages: 13202-13213

Journal: Biochemistry

Volume number: 44

Issue number: 39

ISSN: 0006-2960

DOI Link: https://doi.org/10.1021/bi050906n

Publisher: American Chemical Society

Abstract: 
Phosphorylation of histone H3 is a hallmark event in mitosis and is associated with chromosome condensation. Here, we use a combination of immobilized metal affinity chromatography and tandem mass spectrometry to characterize post-translational modifications associated with phosphorylation on the N-terminal tails of histone H3 variants purified from mitotically arrested HeLa cells. Modifications observed in vivo on lysine residues adjacent to phosphorylated Ser and Thr provide support for the existence of the "methyl/phos", binary-switch hypothesis [Fischle, W., Wang, Y., and Allis, C. D. (2003) Nature 425, 475-479]. ELISA with antibodies selective for H3 at Ser10, Ser28, and Thr3 show reduced activity when adjacent Lys residues are modified. When used together, mass spectrometry and immunoassay methods provide a powerful approach for elucidation of the histone code and identification of histone post-translational modifications that occur during mitosis and other specific cellular events.

Harvard Citation style: Garcia, B., Barber, C., Hake, S., Ptak, C., Turner, F., Busby, S., et al. (2005) Modifications of human histone H3 variants during mitosis, Biochemistry, 44(39), pp. 13202-13213. https://doi.org/10.1021/bi050906n

APA Citation style: Garcia, B., Barber, C., Hake, S., Ptak, C., Turner, F., Busby, S., Shabanowitz, J., Moran, R., Allis, C., & Hunt, D. (2005). Modifications of human histone H3 variants during mitosis. Biochemistry. 44(39), 13202-13213. https://doi.org/10.1021/bi050906n