NASP maintains histone H3-H4 homeostasis through two distinct H3 binding modes

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

NASP maintains histone H3-H4 homeostasis through two distinct H3 binding modes. / Bao, Hongyu; Carraro, Massimo; Flury, Valentin; Liu, Yanhong; Luo, Min; Chen, Liu; Groth, Anja; Huang, Hongda.

In: Nucleic Acids Research, Vol. 50, No. 9, 2022, p. 5349-5368.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Bao, H, Carraro, M, Flury, V, Liu, Y, Luo, M, Chen, L, Groth, A & Huang, H 2022, 'NASP maintains histone H3-H4 homeostasis through two distinct H3 binding modes', Nucleic Acids Research, vol. 50, no. 9, pp. 5349-5368. https://doi.org/10.1093/nar/gkac303

APA

Bao, H., Carraro, M., Flury, V., Liu, Y., Luo, M., Chen, L., Groth, A., & Huang, H. (2022). NASP maintains histone H3-H4 homeostasis through two distinct H3 binding modes. Nucleic Acids Research, 50(9), 5349-5368. https://doi.org/10.1093/nar/gkac303

Vancouver

Bao H, Carraro M, Flury V, Liu Y, Luo M, Chen L et al. NASP maintains histone H3-H4 homeostasis through two distinct H3 binding modes. Nucleic Acids Research. 2022;50(9):5349-5368. https://doi.org/10.1093/nar/gkac303

Author

Bao, Hongyu ; Carraro, Massimo ; Flury, Valentin ; Liu, Yanhong ; Luo, Min ; Chen, Liu ; Groth, Anja ; Huang, Hongda. / NASP maintains histone H3-H4 homeostasis through two distinct H3 binding modes. In: Nucleic Acids Research. 2022 ; Vol. 50, No. 9. pp. 5349-5368.

Bibtex

@article{e625ab4f65c94e63955996ceff361a33,
title = "NASP maintains histone H3-H4 homeostasis through two distinct H3 binding modes",
abstract = "Histone chaperones regulate all aspects of histone metabolism. NASP is a major histone chaperone for H3-H4 dimers critical for preventing histone degradation. Here, we identify two distinct histone binding modes of NASP and reveal how they cooperate to ensure histone H3-H4 supply. We determine the structures of a sNASP dimer, a complex of a sNASP dimer with two H3 α3 peptides, and the sNASP-H3-H4-ASF1b co-chaperone complex. This captures distinct functionalities of NASP and identifies two distinct binding modes involving the H3 α3 helix and the H3 αN region, respectively. Functional studies demonstrate the H3 αN-interaction represents the major binding mode of NASP in cells and shielding of the H3 αN region by NASP is essential in maintaining the H3-H4 histone soluble pool. In conclusion, our studies uncover the molecular basis of NASP as a major H3-H4 chaperone in guarding histone homeostasis.",
author = "Hongyu Bao and Massimo Carraro and Valentin Flury and Yanhong Liu and Min Luo and Liu Chen and Anja Groth and Hongda Huang",
note = "{\textcopyright} The Author(s) 2022. Published by Oxford University Press on behalf of Nucleic Acids Research.",
year = "2022",
doi = "10.1093/nar/gkac303",
language = "English",
volume = "50",
pages = "5349--5368",
journal = "Nucleic Acids Research",
issn = "0305-1048",
publisher = "Oxford University Press",
number = "9",

}

RIS

TY - JOUR

T1 - NASP maintains histone H3-H4 homeostasis through two distinct H3 binding modes

AU - Bao, Hongyu

AU - Carraro, Massimo

AU - Flury, Valentin

AU - Liu, Yanhong

AU - Luo, Min

AU - Chen, Liu

AU - Groth, Anja

AU - Huang, Hongda

N1 - © The Author(s) 2022. Published by Oxford University Press on behalf of Nucleic Acids Research.

PY - 2022

Y1 - 2022

N2 - Histone chaperones regulate all aspects of histone metabolism. NASP is a major histone chaperone for H3-H4 dimers critical for preventing histone degradation. Here, we identify two distinct histone binding modes of NASP and reveal how they cooperate to ensure histone H3-H4 supply. We determine the structures of a sNASP dimer, a complex of a sNASP dimer with two H3 α3 peptides, and the sNASP-H3-H4-ASF1b co-chaperone complex. This captures distinct functionalities of NASP and identifies two distinct binding modes involving the H3 α3 helix and the H3 αN region, respectively. Functional studies demonstrate the H3 αN-interaction represents the major binding mode of NASP in cells and shielding of the H3 αN region by NASP is essential in maintaining the H3-H4 histone soluble pool. In conclusion, our studies uncover the molecular basis of NASP as a major H3-H4 chaperone in guarding histone homeostasis.

AB - Histone chaperones regulate all aspects of histone metabolism. NASP is a major histone chaperone for H3-H4 dimers critical for preventing histone degradation. Here, we identify two distinct histone binding modes of NASP and reveal how they cooperate to ensure histone H3-H4 supply. We determine the structures of a sNASP dimer, a complex of a sNASP dimer with two H3 α3 peptides, and the sNASP-H3-H4-ASF1b co-chaperone complex. This captures distinct functionalities of NASP and identifies two distinct binding modes involving the H3 α3 helix and the H3 αN region, respectively. Functional studies demonstrate the H3 αN-interaction represents the major binding mode of NASP in cells and shielding of the H3 αN region by NASP is essential in maintaining the H3-H4 histone soluble pool. In conclusion, our studies uncover the molecular basis of NASP as a major H3-H4 chaperone in guarding histone homeostasis.

U2 - 10.1093/nar/gkac303

DO - 10.1093/nar/gkac303

M3 - Journal article

C2 - 35489058

VL - 50

SP - 5349

EP - 5368

JO - Nucleic Acids Research

JF - Nucleic Acids Research

SN - 0305-1048

IS - 9

ER -

ID: 305461901