H4 replication-dependent diacetylation and Hat1 promote S-phase chromatin assembly in vivo

Ejlassi-Lassallette, Aïda; Mocquard, Eloïse; Arnaud, Marie-Claire; Thiriet, Christophe

doi:10.1091/mbc.e10-07-0633

Cited by 67 publications

(90 citation statements)

References 61 publications

(129 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…However, H3 and H4 import is likely coordinated with upstream and downstream histone processing/nucleosome assembly events and thus may involve other protein players (28,30,31,(52)(53)(54)(55)(56). Furthermore, H3 and H4 dimerize and bind histone chaperone b before binding FIGURE 4.…”

Section: Discussionmentioning

confidence: 99%

“…Acetylation of H3 Lys 14 Impairs Importin Binding-The Importin-binding segments in H3 and H4 tails contain several lysine residues that are acetylated to different degrees in the cytoplasm (H3 Lys 14 , H3 Lys 18 , H4 Lys 5 , and H4 Lys 12 ) (28,30,31,(52)(53)(54). The role of histone acetylation in nuclear import was controversial with reports of both promoting and inhibiting histone import (12,17,31).…”

Section: Discussionmentioning

confidence: 99%

“…The role of histone acetylation in nuclear import was controversial with reports of both promoting and inhibiting histone import (12,17,31).…”

Section: Discussionmentioning

confidence: 99%

“…Previous studies showed that N-terminal tails of histones H3 and H4 are necessary and sufficient for nuclear import, consistent with the presence of NLS-like sequences in the tails. Removal of either the H3 or H4 tail does not prevent nuclear import, but simultaneous removal of both tails produced non-viable S. cerevisiae and caused loss of nuclear H3-H4 in Physarum polycephalum (12,31). Of the Importins that bind and import H3 and H4, only classes of NLSs for Imp␣/Imp␤, Kap␤2, and Imp5 are known.…”

mentioning

confidence: 99%

“…Mutations of H3 and H4 tail lysines to glutamines (acetylation mimics) in yeast abolished nuclear accumulation, slowed growth, or caused loss of viability, suggesting that acetylation impairs nuclear import (12). In contrast, H3 and H4 acetylation in P. polycephalum led to increased nuclear accumulation, and acetylated H4 tail peptides were reported to bind Imp4 better than unacetylated peptides, suggesting that acetylation may promote nuclear import (17,31).…”

mentioning

confidence: 99%

See 4 more Smart Citations

Recognition Elements in the Histone H3 and H4 Tails for Seven Different Importins

Soniat

Çağatay

Chook

2016

Journal of Biological Chemistry

View full text Add to dashboard Cite

N-terminal tails of histones H3 and H4 are known to bind several different Importins to import the histones into the cell nucleus. However, it is not known what binding elements in the histone tails are recognized by the individual Importins. Biochemical studies of H3 and H4 tails binding to seven Importins, Imp␤, Kap␤2, Imp4, Imp5, Imp7, Imp9, and Imp␣, show the H3 tail binding more tightly than the H4 tail. The H3 tail binds Kap␤2 and Imp5 with K D values of 77 and 57 nM, respectively, and binds the other five Importins more weakly. Mutagenic analysis shows H3 tail residues 11-27 to be the sole binding segment for Imp␤, Kap␤2, and Imp4. However, Imp5, Imp7, Imp9, and Imp␣ bind two separate elements in the H3 tail: the segment at residues 11-27 and an isoleucine-lysine nuclear localization signal (IK-NLS) motif at residues 35-40. The H4 tail also uses either one or two basic segments to bind the same set of Importins with a similar trend of relative affinities as the H3 tail, albeit at least 10-fold weaker. Of the many lysine residues in the H3 and H4 tails, only acetylation of the H3 Lys 14 substantially decreased binding to several Importins. Lastly, we show that, in addition to the N-terminal tails, the histone fold domains of H3 and H4 and/or the histone chaperone Asf1b are important for Importin-histone recognition.New nucleosomes are assembled in the nucleus during S phase as new core histones H2A, H2B, H3, and H4 are synthesized, assembled into H2A/H2B and H3/H4 dimers in the cytoplasm, and then imported into the nucleus for deposition onto replicating chromatin (1-8). Little is known about cytoplasmic assembly/processing of H2A and H2B, but assembly/processing of H3 and H4 are better understood. In the cytoplasm, H3 and H4 are passed from one histone chaperone to another for folding, assembly into H3/H4 dimers, and acetylation.

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

“…The role of histone acetylation in nuclear import was controversial with reports of both promoting and inhibiting histone import (12,17,31).…”

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

See 3 more Smart Citations

Recognition Elements in the Histone H3 and H4 Tails for Seven Different Importins

Soniat

Çağatay

Chook

2016

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

The effects of acetaldehyde exposure on histone modifications and chromatin structure in human lung bronchial epithelial cells

Chen

Fang

et al. 2018

Environ and Mol Mutagen

View full text Add to dashboard Cite

As the primary metabolite of alcohol and the most abundant carcinogen in tobacco smoke, acetaldehyde is linked to a number of human diseases associated with chronic alcohol consumption and smoking including cancers. In addition to direct DNA damage as a result of the formation of acetaldehyde-DNA adducts, acetaldehyde may also indirectly impact proper genome function through the formation of protein adducts. Histone proteins are the major component of the chromatin. Post-translational histone modifications (PTMs) are critically important for the maintenance of genetic and epigenetic stability. However, little is known about how acetaldehyde-histone adducts affect histone modifications and chromatin structure. The results of protein carbonyl assays suggest that acetaldehyde forms adducts with histone proteins in human bronchial epithelial BEAS-2B cells. The level of acetylation for N-terminal tails of cytosolic histones H3 and H4, an important modification for histone nuclear import and chromatin assembly, is significantly downregulated following acetaldehyde exposure in BEAS-2B cells, possibly due to the formation of histone adducts and/or the decrease in the expression of histone acetyltransferases. Notably, the level of nucleosomal histones in the chromatin fraction and at most of the genomic loci we tested are low in acetaldehyde-treated cells as compared with the control cells, which is suggestive of inhibition of chromatin assembly. Moreover, acetaldehyde exposure perturbs chromatin structure as evidenced by the increase in general chromatin accessibility and the decrease in nucleosome occupancy at genomic loci following acetaldehyde treatment. Our results indicate that regulation of histone modifications and chromatin accessibility may play important roles in acetaldehyde-induced pathogenesis. Environ. Mol. Mutagen. 59:375-385, 2018. © 2018 Wiley Periodicals, Inc.

show abstract

Chemical and Biological Tools for the Preparation of Modified Histone Proteins

Howard

Gardner

et al. 2015

Topics in Current Chemistry

View full text Add to dashboard Cite

Eukaryotic chromatin is a complex and dynamic system in which the DNA double helix is organized and protected by interactions with histone proteins. This system is regulated through, a large network of dynamic post-translational modifications (PTMs) exists to ensure proper gene transcription, DNA repair, and other processes involving DNA. Homogenous protein samples with precisely characterized modification sites are necessary to better understand the functions of modified histone proteins. Here, we discuss sets of chemical and biological tools that have been developed for the preparation of modified histones, with a focus on the appropriate choice of tool for a given target. We start with genetic approaches for the creation of modified histones, including the incorporation of genetic mimics of histone modifications, chemical installation of modification analogs, and the use of the expanded genetic code to incorporate modified amino acids. Additionally, we will cover the chemical ligation techniques that have been invaluable in the generation of complex modified histones that are indistinguishable from the natural counterparts. Finally, we will end with a prospectus on future directions of synthetic chromatin in living systems.

show abstract

H4 replication-dependent diacetylation and Hat1 promote S-phase chromatin assembly in vivo

Cited by 67 publications

References 61 publications

Recognition Elements in the Histone H3 and H4 Tails for Seven Different Importins

Recognition Elements in the Histone H3 and H4 Tails for Seven Different Importins

The effects of acetaldehyde exposure on histone modifications and chromatin structure in human lung bronchial epithelial cells

Chemical and Biological Tools for the Preparation of Modified Histone Proteins

Contact Info

Product

Resources

About