Structural characterization of the Asf1–Rtt109 interaction and its role in histone acetylation

Lercher, Lukas; Danilenko, Nataliya; Kirkpatrick, John; Carlomagno, Teresa

doi:10.1093/nar/gkx1283

Cited by 19 publications

(28 citation statements)

References 72 publications

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“…Bottom, the corresponding CSPs plot. In Asf1–H3:H4, the H3 tail interacts with Asf1, as reported by Lercher et al 34 . In the presence of Vps75 2 1–225 , the H3 tail is released from Asf1 and recovers the CSs of the H3:H4 dimer; in the presence of Vps75 2 , the H3 tail peaks move to new positions.…”

Section: Resultssupporting

confidence: 72%

“…5a). CSPs were observed for residues on the surface opposite to that binding the histones, which result from the previously reported interaction with the Rtt109 C-terminal region 34 . The SANS curve of the Asf1–H3 35–135 :H4–Rtt109–Vps75 2 complex acquired in 100% D 2 O buffer, using 1 H-Asf1–H3 35–135 :H4 and 2 H(70%)-Rtt109–Vps75, reported on the conformation of the Asf1–H3:H4 sub-complex within the full complex.…”

Section: Resultssupporting

confidence: 60%

“…Spectra were recorded on samples of 60 μM Vps75 2 in 50 mM sodium citrate pH 6.5, 150 mM NaCl, 5 mM BME at 850 MHz and 298 K. b The Asf1–H3:H4–Rtt109–Vps75 2 complex adopts a doughnut-like shape with a central cavity of ~25 Å width. The Rtt109 C-terminal tail (Rtt109 419–433 ) is shown bound to Asf1, as described in Lercher et al 34 (PDB entry 6f0y). A flat ribbon indicates the portion of the Rtt109 C-terminal tail for which no structural information is available.…”

Section: Resultsmentioning

confidence: 99%

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Histone chaperone exploits intrinsic disorder to switch acetylation specificity

et al. 2019

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Histones, the principal protein components of chromatin, contain long disordered sequences, which are extensively post-translationally modified. Although histone chaperones are known to control both the activity and specificity of histone-modifying enzymes, the mechanisms promoting modification of highly disordered substrates, such as lysine-acetylation within the N-terminal tail of histone H3, are not understood. Here, to understand how histone chaperones Asf1 and Vps75 together promote H3 K9-acetylation, we establish the solution structural model of the acetyltransferase Rtt109 in complex with Asf1 and Vps75 and the histone dimer H3:H4. We show that Vps75 promotes K9-acetylation by engaging the H3 N-terminal tail in fuzzy electrostatic interactions with its disordered C-terminal domain, thereby confining the H3 tail to a wide central cavity faced by the Rtt109 active site. These fuzzy interactions between disordered domains achieve localization of lysine residues in the H3 tail to the catalytic site with minimal loss of entropy, and may represent a common mechanism of enzymatic reactions involving highly disordered substrates.

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Section: Resultssupporting

confidence: 72%

Section: Resultssupporting

confidence: 60%

Section: Resultsmentioning

confidence: 99%

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Histone chaperone exploits intrinsic disorder to switch acetylation specificity

et al. 2019

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“…Asf1 participates in replicationcoupled nucleosome assembly by regulating H3K56ac [121], which is crucial to replication-coupled nucleosome assembly and genome stability [27,37]. The binding of Asf1 to Rtt109 stimulates the activity of the acetylase, leading to the acetylation of the H3 lysine 56 residue [122,123]. RFC recruits Asf1 to DNA containing a templateprimer junction [117].…”

Section: Rfc: Potential Roles In Nucleosome Assembly In Addition To Smentioning

confidence: 99%

The replisome guides nucleosome assembly during DNA replication

Zhang

Feng

2020

Cell Biosci

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Nucleosome assembly during DNA replication is tightly coupled to ongoing DNA synthesis. This process, termed DNA replication-coupled (RC) nucleosome assembly, is essential for chromatin replication and has a great impact on both genome stability maintenance and epigenetic inheritance. This review discusses a set of recent findings regarding the role of replisome components contributing to RC nucleosome assembly. Starting with a brief introduction to the factors involved in nucleosome assembly and some aspects of the architecture of the eukaryotic replisome, we discuss studies from yeast to mammalian cells and the interactions of replisome components with histones and histone chaperones. We describe the proposed functions of replisome components during RC nucleosome assembly and discuss their impacts on histone segregation and implications for epigenetic inheritance.

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“…The dysfunction of CIA/ASF1 would cause severe replication defects and loss of chromatin integrity [38,39]. To achieve its biological function, CIA/ASF1 needs to interact with many other specific macromolecular sites [21,33,40,41]. The site-specific histone eviction from the nucleosome by CIA/ASF1 at the transcription initiation process is generally induced by the histone acetylation around the active promoter region.…”

Section: Introductionmentioning

confidence: 99%

Dynamics and Mechanisms in the Recruitment and Transference of Histone Chaperone CIA/ASF1

Zhang¹,

Tao²,

Huang³

2019

IJMS

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The recruitment and transference of proteins through protein–protein interactions is a general process involved in various biological functions in cells. Despite the importance of this general process, the dynamic mechanism of how proteins are recruited and transferred from one interacting partner to another remains unclear. In this study, we investigated the dynamic mechanisms of recruitment and translocation of histone chaperone CIA/ASF1 for nucleosome disassembly by exploring the conformational space and the free energy profile of unbound DBD(CCG1) and CIA/ASF1-bound DBD(CCG1) systems through extensive molecular dynamics simulations. It was found that there exists three metastable conformational states for DBD(CCG1), an unbound closed state, a CIA/ASF1-bound half-open state, and an open state. The free energy landscape shows that the closed state and the half-open state are separated by a high free energy barrier, while the half-open state and the open state are connected with a moderate free energy increase. The high free energy barrier between the closed and half-open states explains why DBD(CCG1) can recruit CIA/ASF1 and remain in the binding state during the transportation. In addition, the asymmetric binding of CIA/ASF1 on DBD(CCG1) allows DBD(CCG1) to adopt the open state by moving one of its two domains, such that the exposed domain of DBD(CCG1) is able to recognize the acetylated histone H4 tails. As such, CIA/ASF1 has a chance to translocate from DBD(CCG1) to histone, which is also facilitated by the moderate energy increase from the bound half-open state to the open state of DBD(CCG1). These findings suggest that the recruitment and transference of histone chaperone CIA/ASF1 is highly favored by its interaction with DBD(CCG1) via conformational selection and asymmetric binding, which may represent a general mechanism of similar biological processes.

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Structural characterization of the Asf1–Rtt109 interaction and its role in histone acetylation

Cited by 19 publications

References 72 publications

Histone chaperone exploits intrinsic disorder to switch acetylation specificity

Histone chaperone exploits intrinsic disorder to switch acetylation specificity

The replisome guides nucleosome assembly during DNA replication

Dynamics and Mechanisms in the Recruitment and Transference of Histone Chaperone CIA/ASF1

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