DNA-dependent protein kinase catalytic subunit (DNA-PKcs) contributes to incorporation of histone variant H2A.Z into nucleosomes

Ling-Yao Wang, Yun-xiao He, Min Li, Jian Ding, Yi Sui, Joan W. Conaway, Ronald C. Conaway, Fei Wang, Jingji Jin, Yong Cai

PDF(913 KB)
PDF(913 KB)
Protein Cell ›› 2019, Vol. 10 ›› Issue (9) : 694-699. DOI: 10.1007/s13238-019-0632-1
LETTER
LETTER

DNA-dependent protein kinase catalytic subunit (DNA-PKcs) contributes to incorporation of histone variant H2A.Z into nucleosomes

Author information +
History +

Cite this article

Download citation ▾
Ling-Yao Wang, Yun-xiao He, Min Li, Jian Ding, Yi Sui, Joan W. Conaway, Ronald C. Conaway, Fei Wang, Jingji Jin, Yong Cai. DNA-dependent protein kinase catalytic subunit (DNA-PKcs) contributes to incorporation of histone variant H2A.Z into nucleosomes. Protein Cell, 2019, 10(9): 694‒699 https://doi.org/10.1007/s13238-019-0632-1

References

[1]
Alatwi HE, Downs JA (2015) Removal of H2A.Z by INO80 promotes homologous recombination. EMBO Rep 16:986–994
CrossRef Google scholar
[2]
Davis AJ, Chen BP, Chen DJ (2014) DNA-PK: a dynamic enzyme in a versatile DSB repair pathway. DNA Repair (Amst) 17:21–29
CrossRef Google scholar
[3]
Ding J, Yu C, Sui Y, Wang L, Yang Y, Wang F, Yao H, Xing F, Liu H, Li Y (2018) The chromatin remodeling protein INO80 contributes to the removal of H2A.Z at the p53-binding site of the p21 gene in response to doxorubicin. FEBS J 285:3270–3285
CrossRef Google scholar
[4]
Hu G, Cui K, Northrup D, Liu C, Wang C, Tang Q, Ge K, Levens D, Crane-Robinson C, Zhao K (2013) H2A.Z facilitates access of active and repressive complexes to chromatin in embryonic stem cell self-renewal and differentiation. Cell Stem Cell 12:180–192
CrossRef Google scholar
[5]
Lademann CA, Renkawitz J, Pfander B, Jentsch S (2017) The INO80 complex removes H2A.Z to promote presynaptic filament formation during homologous recombination. Cell Rep 19:1294–1303
CrossRef Google scholar
[6]
Littlewood TD, Hancock DC, Danielian PS, Parker MG, Evan GI (1995) A modified oestrogen receptor ligand-binding domain as an improved switch for the regulation of heterologous proteins. Nucleic Acids Res 23:1686–1690
CrossRef Google scholar
[7]
Mao Z, Pan L, Wang W, Sun J, Shan S, Dong Q, Liang X, Dai L, Ding X, Chen S (2014) Anp32e, a higher eukaryotic histone chaperone directs preferential recognition for H2A.Z. Cell Res 24:389–399
CrossRef Google scholar
[8]
Obri A, Ouararhni K, Papin C, Diebold ML, Padmanabhan K, Marek M, Stoll I, Roy L, Reilly PT, Mak TW (2014) ANP32E is a histone chaperone that removes H2A.Z from chromatin. Nature 505:648–653
CrossRef Google scholar
[9]
Papamichos-Chronakis M, Watanabe S, Rando OJ, Peterson CL (2011) Global regulation of H2A.Z localization by the INO80 chromatin-remodeling enzyme is essential for genome integrity. Cell 144:200–213
CrossRef Google scholar
[10]
Qi W, Wang R, Chen H, Wang X, Xiao T, Boldogh I, Ba X, Han L, Zeng X (2015) BRG1 promotes the repair of DNA double-strand breaks by facilitating the replacement of RPA with RAD51. J Cell Sci 128:317–330
CrossRef Google scholar
[11]
Ruhl DD, Jin J, Cai Y, Swanson S, Florens L, Washburn MP, Conaway RC, Conaway JW, Chrivia JC (2006) Purification of a human SRCAP complex that remodels chromatin by incorporating the histone variant H2A.Z into nucleosomes. Biochemistry 45:5671–5677
CrossRef Google scholar
[12]
Shin H, He M, Yang Z, Jeon YH, Pfleger J, Sayed D, Abdellatif M (2018) Transcriptional regulation mediated by H2A.Z via ANP32e-dependent inhibition of protein phosphatase 2A. Biochim Biophys Acta Gene Regul Mech 1861:481–496
CrossRef Google scholar
[13]
Su Y, Wang S, Zhan F, Zheng H, Liu Y, Huang T, Ding Y (2017) Phosphorylation of histone H2A at serine 95: a plant-specific mark involved in flowering time regulation and H2A.Z deposition. Plant Cell 29:2197–2213
CrossRef Google scholar

RIGHTS & PERMISSIONS

2019 The Author(s) 2019
AI Summary AI Mindmap
PDF(913 KB)

Accesses

Citations

Detail

Sections
Recommended

/