Choreography of parental histones in damaged chromatin

Dabin, Juliette; Polo, Sophie E.

doi:10.1080/19491034.2017.1292192

Cited by 5 publications

(4 citation statements)

References 36 publications

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“…The Nap1-binding site of H2A-H2B is accessible in RanGTP•Kap114•H2A-H2B for transfer of the histone to Nap1, or for Nap1 to co-chaperone the histone in a larger RanGTP•Kap114•H2A-H2B•Nap1 assembly. These scenarios are useful to guide future studies of histone biosynthesis in the cytoplasm and nucleosome assembly/disassembly in the nucleus as they resemble multiple known examples of cascades of histone co-chaperoning or transfer between histone chaperones (Elsasser and D’Arcy 2012; Dabin and Polo 2017; Pardal, Fernandes-Duarte, and Bowman 2019; Bernardes et al 2022).…”

Section: Discussionmentioning

confidence: 99%

“…The Nap1-binding site of H2A-H2B overlaps with the N-terminal Kap114-binding site but not the C-terminal binding site (4,38), which may be how Kap114 binds Nap1-bound H2A-H2B. It is unclear whether H2A-H2B is transferred between Nap1 and Kap114 akin to transfers in the histone chaperone network (39)(40)(41)(42) or H2A-H2B is co-chaperoned by Nap1 and Kap114 like in ASF1•H3-H4•Importin-4 (25).…”

Section: Discussionmentioning

confidence: 99%

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Mechanism of RanGTP priming H2A-H2B release from Kap114 in an atypical RanGTP•Kap114•H2A-H2B complex

Jiou

Shaffer²,

Bernardes

et al. 2022

Preprint

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Previously we showed that the nuclear import receptor Importin-9 wraps around the H2A-H2B core to chaperone and transport it from the cytoplasm to the nucleus (Padavannil et al. 2019). However, unlike most nuclear import systems where RanGTP dissociates cargoes from their importins, RanGTP binds stably to the Importin-9•H2A-H2B complex and formation of RanGTP•Importin-9•H2A-H2B facilitates H2A-H2B release to the assembling nucleosome (Padavannil et al. 2019). Here we show cryo-EM structures of Importin-9•RanGTP and of its yeast homolog Kap114, including Kap114•RanGTP, Kap114•H2A-H2B, and RanGTP•Kap114•H2A-H2B. In combination with hydrogen-deuterium exchange analysis of Importin-9 complexes and nucleosome assembly assays, we explain how the conserved Kap114/Importin-9 importins bind H2A-H2B and RanGTP simultaneously and how the GTPase primes histone transfer to the nucleosome. We show that RanGTP binds to the N-terminal repeats of Kap114/Importin-9 as in Kap114/Importin-9•RanGTP, and H2A-H2B binds via its acidic patch to the Kap114/Importin-9 C-terminal repeats as in Kap114/Importin-9•H2A-H2B. RanGTP-binding in RanGTP•Kap114•H2A-H2B changes Kap114/Importin-9 conformation such that it no longer contacts the surface of H2A-H2B proximal to the H2A docking domain that drives nucleosome assembly, positioning it for transfer to the assembling nucleosome. The reduced affinity of RanGTP for Kap114/Importin-9 when H2A-H2B is bound may ensure release of H2A-H2B only at chromatin.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Mechanism of RanGTP priming H2A-H2B release from Kap114 in an atypical RanGTP•Kap114•H2A-H2B complex

Jiou

Shaffer²,

Bernardes

et al. 2022

Preprint

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“…Histone chaperones also play a central role during DNA repair, omitted here for brevity. For a detailed description we refer the reader to some recent excellent reviews [131–133].…”

Section: The Challenges In Observing Transitions Between Histone Chapmentioning

confidence: 99%

The histone chaperoning pathway: from ribosome to nucleosome

Pardal

Fernandes-Duarte

Bowman

2019

Essays in Biochemistry

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Nucleosomes represent the fundamental repeating unit of eukaryotic DNA, and comprise eight core histones around which DNA is wrapped in nearly two superhelical turns. Histones do not have the intrinsic ability to form nucleosomes; rather, they require an extensive repertoire of interacting proteins collectively known as ‘histone chaperones’. At a fundamental level, it is believed that histone chaperones guide the assembly of nucleosomes through preventing non-productive charge-based aggregates between the basic histones and acidic cellular components. At a broader level, histone chaperones influence almost all aspects of chromatin biology, regulating histone supply and demand, governing histone variant deposition, maintaining functional chromatin domains and being co-factors for histone post-translational modifications, to name a few. In this essay we review recent structural insights into histone-chaperone interactions, explore evidence for the existence of a histone chaperoning ‘pathway’ and reconcile how such histone-chaperone interactions may function thermodynamically to assemble nucleosomes and maintain chromatin homeostasis.

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“…To modulate nucleosome properties, including DNA accessibility and interactions between nucleosomes or even chromatin fibers, different histone variants can be incorporated. Recent years have seen accumulating evidence for the functional importance of these different histone variants for processes ranging from gene expression control and reprogramming to DNA repair processes in mammals and plants (Jiang and Berger, 2016;Buschbeck and Hake, 2017;Dabin and Polo, 2017).…”

Section: Session 3: Making Variations Of Chromatin-incorporating Bricmentioning

confidence: 99%

Looking At the Past and Heading to the Future: Meeting Summary of the 6th European Workshop on Plant Chromatin 2019 in Cologne, Germany

et al. 2020

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In June 2019, more than a hundred plant researchers met in Cologne, Germany, for the 6 th European Workshop on Plant Chromatin (EWPC). This conference brought together a highly dynamic community of researchers with the common aim to understand how chromatin organization controls gene expression, development, and plant responses to the environment. New evidence showing how epigenetic states are set, perpetuated, and inherited were presented, and novel data related to the three-dimensional organization of chromatin within the nucleus were discussed. At the level of the nucleosome, its composition by different histone variants and their specialized histone deposition complexes were addressed as well as the mechanisms involved in histone posttranslational modifications and their role in gene expression. The keynote lecture on plant DNA methylation by Julie Law (SALK Institute) and the tribute session to Lars Hennig, honoring the memory of one of the founders of the EWPC who contributed to promote the plant chromatin and epigenetic field in Europe, added a very special note to this gathering. In this perspective article we summarize some of the most outstanding data and advances on plant chromatin research presented at this workshop.

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Choreography of parental histones in damaged chromatin

Cited by 5 publications

References 36 publications

Mechanism of RanGTP priming H2A-H2B release from Kap114 in an atypical RanGTP•Kap114•H2A-H2B complex

Mechanism of RanGTP priming H2A-H2B release from Kap114 in an atypical RanGTP•Kap114•H2A-H2B complex

The histone chaperoning pathway: from ribosome to nucleosome

Looking At the Past and Heading to the Future: Meeting Summary of the 6th European Workshop on Plant Chromatin 2019 in Cologne, Germany

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