scholarly journals NASP maintains histone H3–H4 homeostasis through two distinct H3 binding modes

2021 ◽  
Author(s):  
Hongyu Bao ◽  
Massimo Carraro ◽  
Valentin Flury ◽  
Yanhong Liu ◽  
Min Luo ◽  
...  
Keyword(s):  
Histone H3 ◽  
Histone Chaperone ◽  
Histone Chaperones ◽  
Binding Modes ◽  
Histone Binding ◽  
Chaperone Complex

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 sNASP with an H3 α3 peptide, and the sNASP–H3–H4–ASF1b co-chaperone complex.

scholarly journals Histone transfer among chaperones

2012 ◽  
Vol 40 (2) ◽  
pp. 357-363 ◽  
Author(s):  
Wallace H. Liu ◽  
Mair E.A. Churchill
Keyword(s):  
Histone H3 ◽  
Histone Chaperone ◽  
Chromatin Assembly ◽  
Histone Chaperones ◽  
Nucleosome Assembly ◽  
Post Translational Modifications ◽  
Chromatin Dynamics ◽  
Nucleosomal Dna ◽  
Chaperone Interactions ◽  
Dependent Processes

The eukaryotic processes of nucleosome assembly and disassembly govern chromatin dynamics, in which histones exchange in a highly regulated manner to promote genome accessibility for all DNA-dependent processes. This regulation is partly carried out by histone chaperones, which serve multifaceted roles in co-ordinating the interactions of histone proteins with modification enzymes, nucleosome remodellers, other histone chaperones and nucleosomal DNA. The molecular details of the processes by which histone chaperones promote delivery of histones among their many functional partners are still largely undefined, but promise to offer insights into epigenome maintenance. In the present paper, we review recent findings on the histone chaperone interactions that guide the assembly of histones H3 and H4 into chromatin. This evidence supports the concepts of histone post-translational modifications and specific histone chaperone interactions as guiding principles for histone H3/H4 transactions during chromatin assembly.

scholarly journals Distinct histone H3–H4 binding modes of sNASP reveal the basis for cooperation and competition of histone chaperones

2021 ◽  
Author(s):  
Chao-Pei Liu ◽  
Wenxing Jin ◽  
Jie Hu ◽  
Mingzhu Wang ◽  
Jingjing Chen ◽  
...  
Keyword(s):  
De Novo ◽  
Critical Role ◽  
Histone H3 ◽  
Coiled Coil ◽  
Dynamic Network ◽  
Histone Chaperones ◽  
Binding Modes ◽  
Nucleosome Assembly ◽  
Partially Unfolded

Chromosomal duplication requires de novo assembly of nucleosomes from newly synthesized histones, and the process involves a dynamic network of interactions between histones and histone chaperones. sNASP and ASF1 are two major histone H3–H4 chaperones found in distinct and common complexes, yet how sNASP binds H3–H4 in the presence and absence of ASF1 remains unclear. Here we show that, in the presence of ASF1, sNASP principally recognizes a partially unfolded Nα region of histone H3, and in the absence of ASF1, an additional sNASP binding site becomes available in the core domain of the H3–H4 complex. Our study also implicates a critical role of the C-terminal tail of H4 in the transfer of H3–H4 between sNASP and ASF1 and the coiled-coil domain of sNASP in nucleosome assembly. These findings provide mechanistic insights into coordinated histone binding and transfer by histone chaperones.

scholarly journals Histone chaperone FACT represses retrotransposon MERVL and MERVL-derived cryptic promoters

2020 ◽  
Vol 48 (18) ◽  
pp. 10211-10225 ◽  
Author(s):  
Fuquan Chen ◽  
Weiyu Zhang ◽  
Dan Xie ◽  
Tingting Gao ◽  
Zhiqiang Dong ◽  
...  
Keyword(s):  
Target Genes ◽  
Critical Role ◽  
Histone H3 ◽  
Embryonic Stem ◽  
Histone Chaperone ◽  
Endogenous Retroviruses ◽  
Histone Chaperones ◽  
Cryptic Transcription ◽  
Unique Mechanism ◽  
Cryptic Promoters

Abstract Endogenous retroviruses (ERVs) were usually silenced by various histone modifications on histone H3 variants and respective histone chaperones in embryonic stem cells (ESCs). However, it is still unknown whether chaperones of other histones could repress ERVs. Here, we show that H2A/H2B histone chaperone FACT plays a critical role in silencing ERVs and ERV-derived cryptic promoters in ESCs. Loss of FACT component Ssrp1 activated MERVL whereas the re-introduction of Ssrp1 rescued the phenotype. Additionally, Ssrp1 interacted with MERVL and suppressed cryptic transcription of MERVL-fused genes. Remarkably, Ssrp1 interacted with and recruited H2B deubiquitinase Usp7 to Ssrp1 target genes. Suppression of Usp7 caused similar phenotypes as loss of Ssrp1. Furthermore, Usp7 acted by deubiquitinating H2Bub and thereby repressed the expression of MERVL-fused genes. Taken together, our study uncovers a unique mechanism by which FACT complex silences ERVs and ERV-derived cryptic promoters in ESCs.

scholarly journals Two factor authentication: Asf1 mediates crosstalk between H3 K14 and K56 acetylation

2019 ◽  
Vol 47 (14) ◽  
pp. 7380-7391 ◽  
Author(s):  
Joy M Cote ◽  
Yin-Ming Kuo ◽  
Ryan A Henry ◽  
Hataichanok Scherman ◽  
Daniel D Krzizike ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Dna Repair ◽  
Histone Acetylation ◽  
Histone H3 ◽  
Histone Chaperone ◽  
Biochemical Data ◽  
Genome Replication ◽  
Histone Chaperones ◽  
Post Translational Modifications ◽  
Lysine Acetyltransferase

Abstract The ability of histone chaperone Anti-silencing factor 1 (Asf1) to direct acetylation of lysine 56 of histone H3 (H3K56ac) represents an important regulatory step in genome replication and DNA repair. In Saccharomyces cerevisiae, Asf1 interacts functionally with a second chaperone, Vps75, and the lysine acetyltransferase (KAT) Rtt109. Both Asf1 and Vps75 can increase the specificity of histone acetylation by Rtt109, but neither alter selectivity. However, changes in acetylation selectivity have been observed in histones extracted from cells, which contain a plethora of post-translational modifications. In the present study, we use a series of singly acetylated histones to test the hypothesis that histone pre-acetylation and histone chaperones function together to drive preferential acetylation of H3K56. We show that pre-acetylated H3K14ac/H4 functions with Asf1 to drive specific acetylation of H3K56 by Rtt109–Vps75. Additionally, we identified an exosite containing an acidic patch in Asf1 and show that mutations to this region alter Asf1-mediated crosstalk that changes Rtt109–Vps75 selectivity. Our proposed mechanism suggests that Gcn5 acetylates H3K14, recruiting remodeler complexes, allowing for the Asf1-H3K14ac/H4 complex to be acetylated at H3K56 by Rtt109–Vps75. This mechanism explains the conflicting biochemical data and the genetic links between Rtt109, Vps75, Gcn5 and Asf1 in the acetylation of H3K56.

scholarly journals Wie das Histon-Chaperon FACT aktives und stilles Chromatin bewahrt

BIOspektrum ◽  
2021 ◽  
Vol 27 (3) ◽  
pp. 265-268
Author(s):  
Magdalena Murawska ◽  
Andreas G. Ladurner
Keyword(s):  
Histone Chaperone ◽  
Histone Chaperones ◽  
Histone Proteins ◽  
Genome Dynamics ◽  
Chaperone Complex

AbstractHistone chaperones play a fundamental role in the regulation of genome dynamics and stability. They are a versatile group of proteins that interact with histone proteins and govern their assembly or disassembly into nucleosomes. How the activity of histone chaperones is regulated is not well understood. Here, we discuss our new data on how histone post-transcriptional modifications cooperate with the essential histone chaperone complex FACT in active and silent regions of the genome.

scholarly journals The box C/D snoRNP assembly factor Bcd1 interacts with the histone chaperone Rtt106 and controls its transcription dependent activity

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Benoît Bragantini ◽  
Christophe Charron ◽  
Maxime Bourguet ◽  
Arnaud Paul ◽  
Decebal Tiotiu ◽  
...  
Keyword(s):  
Rna Polymerase Ii ◽  
Histone H3 ◽  
Histone Chaperone ◽  
Genetic Interactions ◽  
X Ray ◽  
X Ray Crystallography ◽  
Dependent Activity ◽  
Interaction Interface ◽  
Assembly Factor ◽  
Encoding Gene

AbstractBiogenesis of eukaryotic box C/D small nucleolar ribonucleoproteins initiates co-transcriptionally and requires the action of the assembly machinery including the Hsp90/R2TP complex, the Rsa1p:Hit1p heterodimer and the Bcd1 protein. We present genetic interactions between the Rsa1p-encoding gene and genes involved in chromatin organization including RTT106 that codes for the H3-H4 histone chaperone Rtt106p controlling H3K56ac deposition. We show that Bcd1p binds Rtt106p and controls its transcription-dependent recruitment by reducing its association with RNA polymerase II, modulating H3K56ac levels at gene body. We reveal the 3D structures of the free and Rtt106p-bound forms of Bcd1p using nuclear magnetic resonance and X-ray crystallography. The interaction is also studied by a combination of biophysical and proteomic techniques. Bcd1p interacts with a region that is distinct from the interaction interface between the histone chaperone and histone H3. Our results are evidence for a protein interaction interface for Rtt106p that controls its transcription-associated activity.

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

2021 ◽  
Author(s):  
Ann K Hogan ◽  
Kizhakke M Sathyan ◽  
Alexander B Willis ◽  
Sakshi Khurana ◽  
Shashank Srivastava ◽  
...  
Keyword(s):  
Histone H3 ◽  
Histone Chaperone ◽  
Nucleosomal Histone

scholarly journals A Genome-Wide Screen Reveals a Role for the HIR Histone Chaperone Complex in Preventing Mislocalization of Budding Yeast CENP-A

Genetics ◽  
2018 ◽  
Vol 210 (1) ◽  
pp. 203-218 ◽  
Author(s):  
Sultan Ciftci-Yilmaz ◽  
Wei-Chun Au ◽  
Prashant K. Mishra ◽  
Jessica R. Eisenstatt ◽  
Joy Chang ◽  
...  
Keyword(s):  
Budding Yeast ◽  
Histone Chaperone ◽  
Genome Wide ◽  
A Genome ◽  
Chaperone Complex

scholarly journals The Carboxyl Terminus of Rtt109 Functions in Chaperone Control of Histone Acetylation

2013 ◽  
Vol 12 (5) ◽  
pp. 654-664 ◽  
Author(s):  
Ernest Radovani ◽  
Matthew Cadorin ◽  
Tahireh Shams ◽  
Suzan El-Rass ◽  
Abdel R. Karsou ◽  
...  
Keyword(s):  
Histone Acetyltransferase ◽  
Histone H3 ◽  
Chromatin Assembly ◽  
Carboxyl Terminus ◽  
Histone Chaperones ◽  
Content Type ◽  
Histone H3 Acetylation ◽  
H3 Acetylation

ABSTRACT Rtt109 is a fungal histone acetyltransferase (HAT) that catalyzes histone H3 acetylation functionally associated with chromatin assembly. Rtt109-mediated H3 acetylation involves two histone chaperones, Asf1 and Vps75. In vivo , Rtt109 requires both chaperones for histone H3 lysine 9 acetylation (H3K9ac) but only Asf1 for full H3K56ac. In vitro , Rtt109-Vps75 catalyzes both H3K9ac and H3K56ac, whereas Rtt109-Asf1 catalyzes only H3K56ac. In this study, we extend the in vitro chaperone-associated substrate specificity of Rtt109 by showing that it acetylates vertebrate linker histone in the presence of Vps75 but not Asf1. In addition, we demonstrate that in Saccharomyces cerevisiae a short basic sequence at the carboxyl terminus of Rtt109 (Rtt109C) is required for H3K9ac in vivo . Furthermore, through in vitro and in vivo studies, we demonstrate that Rtt109C is required for optimal H3K56ac by the HAT in the presence of full-length Asf1. When Rtt109C is absent, Vps75 becomes important for H3K56ac by Rtt109 in vivo . In addition, we show that lysine 290 (K290) in Rtt109 is required in vivo for Vps75 to enhance the activity of the HAT. This is the first in vivo evidence for a role for Vps75 in H3K56ac. Taken together, our results contribute to a better understanding of chaperone control of Rtt109-mediated H3 acetylation.

scholarly journals Structure of the human histone chaperone FACT Spt16 N-terminal domain

2016 ◽  
Vol 72 (2) ◽  
pp. 121-128 ◽  
Author(s):  
G. Marcianò ◽  
D. T. Huang
Keyword(s):  
Crystal Structure ◽  
Saccharomyces Cerevisiae ◽  
Complex Surface ◽  
Histone Chaperone ◽  
Titration Calorimetry ◽  
Nucleosome Assembly ◽  
Surface Residue ◽  
Histone Binding ◽  
Terminal Domain ◽  
Heterodimeric Complex

The histone chaperone FACT plays an important role in facilitating nucleosome assembly and disassembly during transcription. FACT is a heterodimeric complex consisting of Spt16 and SSRP1. The N-terminal domain of Spt16 resembles an inactive aminopeptidase. How this domain contributes to the histone chaperone activity of FACT remains elusive. Here, the crystal structure of the N-terminal domain (NTD) of human Spt16 is reported at a resolution of 1.84 Å. The structure adopts an aminopeptidase-like fold similar to those of theSaccharomyces cerevisiaeandSchizosaccharomyces pombeSpt16 NTDs. Isothermal titration calorimetry analyses show that human Spt16 NTD binds histones H3/H4 with low-micromolar affinity, suggesting that Spt16 NTD may contribute to histone binding in the FACT complex. Surface-residue conservation and electrostatic analysis reveal a conserved acidic patch that may be involved in histone binding.

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