Structural basis of H2A.Z recognition by SRCAP chromatin-remodeling subunit YL1 (Q27704247)

7

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1 June 2020

Xuehui Liu

12

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1 June 2020

Zheng Zhou

17

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1 June 2020

author name string

Xiaoping Liang

1

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1 June 2020

Shan Shan

2

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1 June 2020

Lu Pan

3

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1 June 2020

Jicheng Zhao

4

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1 June 2020

Anand Ranjan

5

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1 June 2020

Feng Wang

6

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1 June 2020

Yingzi Huang

8

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1 June 2020

Hanqiao Feng

9

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1 June 2020

Debbie Wei

10

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1 June 2020

Li Huang

11

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1 June 2020

Qiang Zhong

13

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Jizhong Lou

14

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Guohong Li

15

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1 June 2020

Carl Wu

16

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Nature Structural & Molecular Biology

1 June 2020

publication date

April 2016

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published in

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volume

23

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1 June 2020

page(s)

317-323

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1 June 2020

issue

4

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A protein complex containing the conserved Swi2/Snf2-related ATPase Swr1p deposits histone variant H2A.Z into euchromatin

1 June 2020

cites work

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ATP-driven exchange of histone H2AZ variant catalyzed by SWR1 chromatin remodeling complex

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A Snf2 family ATPase complex required for recruitment of the histone H2A variant Htz1.

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Stepwise histone replacement by SWR1 requires dual activation with histone H2A.Z and canonical nucleosome

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Swc2 is a widely conserved H2AZ-binding module essential for ATP-dependent histone exchange

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N terminus of Swr1 binds to histone H2AZ and provides a platform for subunit assembly in the chromatin remodeling complex

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Chz1, a nuclear chaperone for histone H2AZ.

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ANP32E is a histone chaperone that removes H2A.Z from chromatin

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Anp32e, a higher eukaryotic histone chaperone directs preferential recognition for H2A.Z

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The Catalytic Subunit of the SWR1 Remodeler Is a Histone Chaperone for the H2A.Z-H2B Dimer

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NMR structure of chaperone Chz1 complexed with histones H2A.Z-H2B

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Crystal structure of a nucleosome core particle containing the variant histone H2A.Z

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Nucleosome-free region dominates histone acetylation in targeting SWR1 to promoters for H2A.Z replacement

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FACT Disrupts Nucleosome Structure by Binding H2A-H2B with Conserved Peptide Motifs

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Identifiers

DOI

10.1038/NSMB.3190

1 reference

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Dimensions Publication ID

1 June 2020

0 references

1 reference

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