CAF-1-induced oligomerization of histones H3/H4 and mutually exclusive interactions with Asf1 guide H3/H4 transitions among histone chaperones and DNA

Liu, Wallace H.; Roemer, Sarah C.; Port, Alex M.; Churchill, Mair E. A.

doi:10.1093/nar/gks906

Cited by 80 publications

(101 citation statements)

References 53 publications

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“…For example, it will be informative to determine structurally exactly how Vps75 physically interacts with H3. In addition, it will be informative to clarify the relative contribution of Rtt109-Vps75's cytoplasmic and nuclear roles (60) and the in vivo contribution of the Asf1 C terminus to CAF-1 (and other possible) interaction(s) that exist (36).…”

Section: Discussionmentioning

confidence: 99%

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

et al. 2013

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e 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.

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Section: Discussionmentioning

confidence: 99%

“…In yeast the non-evolutionarily conserved carboxyl terminus of Asf1 is extremely acidic, whereas in humans the region is subject to cell cycle-dependent phosphorylation (33). In S. cerevisiae, functions of the Asf1 C terminus include mediating telomeric silencing (34) and physical interactions with Rad53 (35) and CAF-1 (36).…”

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confidence: 99%

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

et al. 2013

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“…Therefore, Acr-ASF1B adducts or Acr-histone adducts themselves may have no effects on the associations in cells exposed to 100 M Acr. However, reduction of H4K5,12 acetylations due to the formation of Acr adducts might have an impact on the interaction because it has been shown that these modifications are required for the association of histones with ASF1B and importin 4 (31,33,46). To test this possibility, we first established BEAS-2B cells stably expressing FLAG-tagged H3 and determined the levels of H3-interacting proteins before and after Acr exposure by FLAG IP, followed by Western blotting assays.…”

Section: Resultsmentioning

confidence: 99%

“…First, some acetylations, such as H4K5,12ac, are required for the association of histones with translocator protein importin 4 and histone chaperone ASF1 to affect histone nuclear translocation and histone transfer (45,46). Second, the modifications may directly affect chromatin assembly processes by facilitating the deposition of histones to DNA and/or Plasmid supercoiling was not affected by the exposure of either histones or ASF1B to Acr.…”

Section: Discussionmentioning

confidence: 99%

“…After acetylation, the histones are bound to ASF1, which associates with importin 4. Thus, downregulation of H4K12ac may disrupt the association of H3/H4 with ASF1 and importin 4, inhibiting histone nuclear translocation (28,45,46). After nuclear import, the H3-H4 dimer of the ASF1 complex is transferred to the central histone chaperone CAF-1, which binds two H3-H4 dimers to form (H3-H4) 2 tetramers and deposits them onto replicating DNA through the CAF-1-proliferating cell nuclear antigen interaction (47,48).…”

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confidence: 99%

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Mechanisms Underlying Acrolein-Mediated Inhibition of Chromatin Assembly

Fang

Chen

et al. 2016

Molecular and Cellular Biology

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Acrolein is a major component of cigarette smoke and cooking fumes. Previously, we reported that acrolein compromises chromatin assembly; however, underlying mechanisms have not been defined. Here, we report that acrolein reacts with lysine residues, including lysines 5 and 12, sites important for chromatin assembly, on histone H4 in vitro and in vivo. Acrolein-modified histones are resistant to acetylation, suggesting that the reduced H4K12 acetylation that occurs following acrolein exposure is probably due to the formation of acrolein-histone lysine adducts. Accordingly, the association of H3/H4 with the histone chaperone ASF1 and importin 4 is disrupted and the translocation of green fluorescent protein-tagged H3 is inhibited in cells exposed to acrolein. Interestingly, in vitro plasmid supercoiling assays revealed that treatment of either histones or ASF1 with acrolein has no effect on the formation of plasmid supercoiling, indicating that acrolein-protein adduct formation itself does not directly interfere with nucleosome assembly. Notably, exposure of histones to acrolein prior to histone acetylation leads to the inhibition of remodeling and spacing factor chromatin assembly, which requires acetylated histones for efficient assembly. These results suggest that acrolein compromises chromatin assembly by reacting with histone lysine residues at the sites critical for chromatin assembly and prevents these sites from physiological modifications.

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Histone Chaperones, Epigenetics, and Cancer

Rafiei

Bremner

2013

Systems Analysis of Chromatin-Related Protein Complexes in Cancer

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CAF-1-induced oligomerization of histones H3/H4 and mutually exclusive interactions with Asf1 guide H3/H4 transitions among histone chaperones and DNA

Cited by 80 publications

References 53 publications

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

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

Mechanisms Underlying Acrolein-Mediated Inhibition of Chromatin Assembly

Histone Chaperones, Epigenetics, and Cancer

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