UBR7 acts as a histone chaperone for post-nucleosomal histone H3

Ann K. Hogan; Kizhakke M. Sathyan; Alexander B. Willis; Sakshi Khurana; Shashank Srivastava; Ewelina Zasadzińska; Alexander S. Lee; Aaron O. Bailey; Matthew N. Gaynes; Jiehuan Huang; Justin Bodner; Celeste D. Rosencrance; Kelvin A. Wong; Marc A. Morgan; Kyle P. Eagen; Ali Shilatifard; Daniel R. Foltz

doi:10.15252/embj.2021108307

UBR7 acts as a histone chaperone for post-nucleosomal histone H3

Ann K. Hogan, Kizhakke M. Sathyan^*, Alexander B. Willis, Sakshi Khurana, Shashank Srivastava, Ewelina Zasadzińska, Alexander S. Lee, Aaron O. Bailey, Matthew N. Gaynes, Jiehuan Huang, Justin Bodner, Celeste D. Rosencrance, Kelvin A. Wong, Marc A. Morgan, Kyle P. Eagen, Ali Shilatifard, Daniel R. Foltz^*

^*Corresponding author for this work

Biochemistry and Molecular Genetics

Research output: Contribution to journal › Article › peer-review

12 Scopus citations

Abstract

Histone chaperones modulate the stability of histones beginning from histone synthesis, through incorporation into DNA, and during recycling during transcription and replication. Following histone removal from DNA, chaperones regulate histone storage and degradation. Here, we demonstrate that UBR7 is a histone H3.1 chaperone that modulates the supply of pre-existing post-nucleosomal histone complexes. We demonstrate that UBR7 binds to post-nucleosomal H3K4me3 and H3K9me3 histones via its UBR box and PHD. UBR7 binds to the non-nucleosomal histone chaperone NASP. In the absence of UBR7, the pool of NASP-bound post-nucleosomal histones accumulate and chromatin is depleted of H3K4me3-modified histones. We propose that the interaction of UBR7 with NASP and histones opposes the histone storage functions of NASP and that UBR7 promotes reincorporation of post-nucleosomal H3 complexes.

Original language	English (US)
Article number	e108307
Journal	EMBO Journal
Volume	40
Issue number	24
DOIs	https://doi.org/10.15252/embj.2021108307
State	Published - Dec 15 2021

Keywords

NASP
UBR7
chaperone
chromatin
histone

ASJC Scopus subject areas

General Immunology and Microbiology
General Biochemistry, Genetics and Molecular Biology
Molecular Biology
General Neuroscience

Access to Document

10.15252/embj.2021108307

Cite this

Hogan, A. K., Sathyan, K. M., Willis, A. B., Khurana, S., Srivastava, S., Zasadzińska, E., Lee, A. S., Bailey, A. O., Gaynes, M. N., Huang, J., Bodner, J., Rosencrance, C. D., Wong, K. A., Morgan, M. A., Eagen, K. P., Shilatifard, A., & Foltz, D. R. (2021). UBR7 acts as a histone chaperone for post-nucleosomal histone H3. EMBO Journal, 40(24), Article e108307. https://doi.org/10.15252/embj.2021108307

@article{c9c7e5e4c1cc4876a06e3bb9471b7798,

title = "UBR7 acts as a histone chaperone for post-nucleosomal histone H3",

abstract = "Histone chaperones modulate the stability of histones beginning from histone synthesis, through incorporation into DNA, and during recycling during transcription and replication. Following histone removal from DNA, chaperones regulate histone storage and degradation. Here, we demonstrate that UBR7 is a histone H3.1 chaperone that modulates the supply of pre-existing post-nucleosomal histone complexes. We demonstrate that UBR7 binds to post-nucleosomal H3K4me3 and H3K9me3 histones via its UBR box and PHD. UBR7 binds to the non-nucleosomal histone chaperone NASP. In the absence of UBR7, the pool of NASP-bound post-nucleosomal histones accumulate and chromatin is depleted of H3K4me3-modified histones. We propose that the interaction of UBR7 with NASP and histones opposes the histone storage functions of NASP and that UBR7 promotes reincorporation of post-nucleosomal H3 complexes.",

keywords = "NASP, UBR7, chaperone, chromatin, histone",

author = "Hogan, {Ann K.} and Sathyan, {Kizhakke M.} and Willis, {Alexander B.} and Sakshi Khurana and Shashank Srivastava and Ewelina Zasadzi{\'n}ska and Lee, {Alexander S.} and Bailey, {Aaron O.} and Gaynes, {Matthew N.} and Jiehuan Huang and Justin Bodner and Rosencrance, {Celeste D.} and Wong, {Kelvin A.} and Morgan, {Marc A.} and Eagen, {Kyle P.} and Ali Shilatifard and Foltz, {Daniel R.}",

note = "Publisher Copyright: {\textcopyright} 2021 The Authors",

year = "2021",

month = dec,

day = "15",

doi = "10.15252/embj.2021108307",

language = "English (US)",

volume = "40",

journal = "EMBO Journal",

issn = "0261-4189",

publisher = "EMBO Press",

number = "24",

}

TY - JOUR

T1 - UBR7 acts as a histone chaperone for post-nucleosomal histone H3

AU - Hogan, Ann K.

AU - Sathyan, Kizhakke M.

AU - Willis, Alexander B.

AU - Khurana, Sakshi

AU - Srivastava, Shashank

AU - Zasadzińska, Ewelina

AU - Lee, Alexander S.

AU - Bailey, Aaron O.

AU - Gaynes, Matthew N.

AU - Huang, Jiehuan

AU - Bodner, Justin

AU - Rosencrance, Celeste D.

AU - Wong, Kelvin A.

AU - Morgan, Marc A.

AU - Eagen, Kyle P.

AU - Shilatifard, Ali

AU - Foltz, Daniel R.

PY - 2021/12/15

Y1 - 2021/12/15

N2 - Histone chaperones modulate the stability of histones beginning from histone synthesis, through incorporation into DNA, and during recycling during transcription and replication. Following histone removal from DNA, chaperones regulate histone storage and degradation. Here, we demonstrate that UBR7 is a histone H3.1 chaperone that modulates the supply of pre-existing post-nucleosomal histone complexes. We demonstrate that UBR7 binds to post-nucleosomal H3K4me3 and H3K9me3 histones via its UBR box and PHD. UBR7 binds to the non-nucleosomal histone chaperone NASP. In the absence of UBR7, the pool of NASP-bound post-nucleosomal histones accumulate and chromatin is depleted of H3K4me3-modified histones. We propose that the interaction of UBR7 with NASP and histones opposes the histone storage functions of NASP and that UBR7 promotes reincorporation of post-nucleosomal H3 complexes.

AB - Histone chaperones modulate the stability of histones beginning from histone synthesis, through incorporation into DNA, and during recycling during transcription and replication. Following histone removal from DNA, chaperones regulate histone storage and degradation. Here, we demonstrate that UBR7 is a histone H3.1 chaperone that modulates the supply of pre-existing post-nucleosomal histone complexes. We demonstrate that UBR7 binds to post-nucleosomal H3K4me3 and H3K9me3 histones via its UBR box and PHD. UBR7 binds to the non-nucleosomal histone chaperone NASP. In the absence of UBR7, the pool of NASP-bound post-nucleosomal histones accumulate and chromatin is depleted of H3K4me3-modified histones. We propose that the interaction of UBR7 with NASP and histones opposes the histone storage functions of NASP and that UBR7 promotes reincorporation of post-nucleosomal H3 complexes.

KW - NASP

KW - UBR7

KW - chaperone

KW - chromatin

KW - histone

UR - http://www.scopus.com/inward/record.url?scp=85119051900&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85119051900&partnerID=8YFLogxK

U2 - 10.15252/embj.2021108307

DO - 10.15252/embj.2021108307

M3 - Article

C2 - 34786730

AN - SCOPUS:85119051900

SN - 0261-4189

VL - 40

JO - EMBO Journal

JF - EMBO Journal

IS - 24

M1 - e108307

ER -

UBR7 acts as a histone chaperone for post-nucleosomal histone H3

Abstract

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this