Protein & Cell >

2019 , Vol. 10 >Issue 9: 694 - 699

DOI: https://doi.org/10.1007/s13238-019-0632-1

LETTER

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

  • Ling-Yao Wang 1 ,
  • Yun-xiao He 1 ,
  • Min Li 1 ,
  • Jian Ding 1 ,
  • Yi Sui 1 ,
  • Joan W. Conaway 2 ,
  • Ronald C. Conaway 2 ,
  • Fei Wang 1 ,
  • Jingji Jin , 1,3,4 ,
  • Yong Cai , 1,3,4
Expand
  • 1. School of Life Sciences, Jilin University, Changchun 130012, China
  • 2. Stowers Institute for Medical Research, 1000E 50th Street, Kansas City, MO 64110, USA
  • 3. National Engineering Laboratory for AIDS Vaccine, Jilin University, Changchun 130012, China
  • 4. Key Laboratory for Molecular Enzymology and Engineering, The Ministry of Education, Jilin University, Changchun 130012, China

Published date: 15 Sep 2019

Copyright

2019 The Author(s) 2019
Fold

Cite this article

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[J]. Protein & Cell, 2019 , 10(9) : 694 -699 . DOI: 10.1007/s13238-019-0632-1

References

Publishing order | Descend order by publishing year | Descend order by cited within
1
Alatwi HE, Downs JA (2015) Removal of H2A.Z by INO80 promotes homologous recombination. EMBO Rep 16:986–994

DOI

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

DOI

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

DOI

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

DOI

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

DOI

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

DOI

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

DOI

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

DOI

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

DOI

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

DOI

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

DOI

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

DOI

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

DOI

Options
Outlines

/

〈 〉