DNAJC9 integrates heat shock molecular chaperones into the histone chaperone network

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

Standard

DNAJC9 integrates heat shock molecular chaperones into the histone chaperone network. / Hammond, Colin M; Bao, Hongyu; Hendriks, Ivo A; Carraro, Massimo; García-Nieto, Alberto; Liu, Yanhong; Reverón-Gómez, Nazaret; Spanos, Christos; Chen, Liu; Rappsilber, Juri; Nielsen, Michael L; Patel, Dinshaw J; Huang, Hongda; Groth, Anja.

In: Molecular Cell, Vol. 81, No. 12, 2021, p. 2533-2548.

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

Harvard

Hammond, CM, Bao, H, Hendriks, IA, Carraro, M, García-Nieto, A, Liu, Y, Reverón-Gómez, N, Spanos, C, Chen, L, Rappsilber, J, Nielsen, ML, Patel, DJ, Huang, H & Groth, A 2021, 'DNAJC9 integrates heat shock molecular chaperones into the histone chaperone network', Molecular Cell, vol. 81, no. 12, pp. 2533-2548. https://doi.org/10.1016/j.molcel.2021.03.041

APA

Hammond, C. M., Bao, H., Hendriks, I. A., Carraro, M., García-Nieto, A., Liu, Y., Reverón-Gómez, N., Spanos, C., Chen, L., Rappsilber, J., Nielsen, M. L., Patel, D. J., Huang, H., & Groth, A. (2021). DNAJC9 integrates heat shock molecular chaperones into the histone chaperone network. Molecular Cell, 81(12), 2533-2548. https://doi.org/10.1016/j.molcel.2021.03.041

Vancouver

Hammond CM, Bao H, Hendriks IA, Carraro M, García-Nieto A, Liu Y et al. DNAJC9 integrates heat shock molecular chaperones into the histone chaperone network. Molecular Cell. 2021;81(12):2533-2548. https://doi.org/10.1016/j.molcel.2021.03.041

Author

Hammond, Colin M ; Bao, Hongyu ; Hendriks, Ivo A ; Carraro, Massimo ; García-Nieto, Alberto ; Liu, Yanhong ; Reverón-Gómez, Nazaret ; Spanos, Christos ; Chen, Liu ; Rappsilber, Juri ; Nielsen, Michael L ; Patel, Dinshaw J ; Huang, Hongda ; Groth, Anja. / DNAJC9 integrates heat shock molecular chaperones into the histone chaperone network. In: Molecular Cell. 2021 ; Vol. 81, No. 12. pp. 2533-2548.

Bibtex

@article{ae82f2b543fb436eaf09384c162ac7c9,
title = "DNAJC9 integrates heat shock molecular chaperones into the histone chaperone network",
abstract = "From biosynthesis to assembly into nucleosomes, histones are handed through a cascade of histone chaperones, which shield histones from non-specific interactions. Whether mechanisms exist to safeguard the histone fold during histone chaperone handover events or to release trapped intermediates is unclear. Using structure-guided and functional proteomics, we identify and characterize a histone chaperone function of DNAJC9, a heat shock co-chaperone that promotes HSP70-mediated catalysis. We elucidate the structure of DNAJC9, in a histone H3-H4 co-chaperone complex with MCM2, revealing how this dual histone and heat shock co-chaperone binds histone substrates. We show that DNAJC9 recruits HSP70-type enzymes via its J domain to fold histone H3-H4 substrates: upstream in the histone supply chain, during replication- and transcription-coupled nucleosome assembly, and to clean up spurious interactions. With its dual functionality, DNAJC9 integrates ATP-resourced protein folding into the histone supply pathway to resolve aberrant intermediates throughout the dynamic lives of histones.",
author = "Hammond, {Colin M} and Hongyu Bao and Hendriks, {Ivo A} and Massimo Carraro and Alberto Garc{\'i}a-Nieto and Yanhong Liu and Nazaret Rever{\'o}n-G{\'o}mez and Christos Spanos and Liu Chen and Juri Rappsilber and Nielsen, {Michael L} and Patel, {Dinshaw J} and Hongda Huang and Anja Groth",
year = "2021",
doi = "10.1016/j.molcel.2021.03.041",
language = "English",
volume = "81",
pages = "2533--2548",
journal = "Molecular Cell",
issn = "1097-2765",
publisher = "Cell Press",
number = "12",

}

RIS

TY - JOUR

T1 - DNAJC9 integrates heat shock molecular chaperones into the histone chaperone network

AU - Hammond, Colin M

AU - Bao, Hongyu

AU - Hendriks, Ivo A

AU - Carraro, Massimo

AU - García-Nieto, Alberto

AU - Liu, Yanhong

AU - Reverón-Gómez, Nazaret

AU - Spanos, Christos

AU - Chen, Liu

AU - Rappsilber, Juri

AU - Nielsen, Michael L

AU - Patel, Dinshaw J

AU - Huang, Hongda

AU - Groth, Anja

PY - 2021

Y1 - 2021

N2 - From biosynthesis to assembly into nucleosomes, histones are handed through a cascade of histone chaperones, which shield histones from non-specific interactions. Whether mechanisms exist to safeguard the histone fold during histone chaperone handover events or to release trapped intermediates is unclear. Using structure-guided and functional proteomics, we identify and characterize a histone chaperone function of DNAJC9, a heat shock co-chaperone that promotes HSP70-mediated catalysis. We elucidate the structure of DNAJC9, in a histone H3-H4 co-chaperone complex with MCM2, revealing how this dual histone and heat shock co-chaperone binds histone substrates. We show that DNAJC9 recruits HSP70-type enzymes via its J domain to fold histone H3-H4 substrates: upstream in the histone supply chain, during replication- and transcription-coupled nucleosome assembly, and to clean up spurious interactions. With its dual functionality, DNAJC9 integrates ATP-resourced protein folding into the histone supply pathway to resolve aberrant intermediates throughout the dynamic lives of histones.

AB - From biosynthesis to assembly into nucleosomes, histones are handed through a cascade of histone chaperones, which shield histones from non-specific interactions. Whether mechanisms exist to safeguard the histone fold during histone chaperone handover events or to release trapped intermediates is unclear. Using structure-guided and functional proteomics, we identify and characterize a histone chaperone function of DNAJC9, a heat shock co-chaperone that promotes HSP70-mediated catalysis. We elucidate the structure of DNAJC9, in a histone H3-H4 co-chaperone complex with MCM2, revealing how this dual histone and heat shock co-chaperone binds histone substrates. We show that DNAJC9 recruits HSP70-type enzymes via its J domain to fold histone H3-H4 substrates: upstream in the histone supply chain, during replication- and transcription-coupled nucleosome assembly, and to clean up spurious interactions. With its dual functionality, DNAJC9 integrates ATP-resourced protein folding into the histone supply pathway to resolve aberrant intermediates throughout the dynamic lives of histones.

U2 - 10.1016/j.molcel.2021.03.041

DO - 10.1016/j.molcel.2021.03.041

M3 - Journal article

C2 - 33857403

VL - 81

SP - 2533

EP - 2548

JO - Molecular Cell

JF - Molecular Cell

SN - 1097-2765

IS - 12

ER -

ID: 261516406