Contribution of histone N‐terminal tails to the structure and stability of nucleosomes

Iwasaki, W.; Miya, Yuta; Horikoshi, Naoki; Osakabe, Akihisa; Taguchi, Hiroyuki; Tachiwana, Hiroaki; Shibata, Takehiko; Kagawa, Wataru; Kurumizaka, Hitoshi

doi:10.1016/j.fob.2013.08.007

Cited by 118 publications

(105 citation statements)

References 53 publications

(91 reference statements)

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“…Histone proteins give the genome the ability to pack very large amounts of DNA in a very small space, but at the same time they leave their N-terminal tails flexible [15]. The N-terminal tail of the histone proteins can undergo post-translational modification by enzymes, adding chemical modifications such as acetylation, methylation, phosphorylation and deamination that alter the structure of the DNA package and allow or prevent gene transcription [16].…”

Section: Discussionmentioning

confidence: 99%

Histone H3 Acetyl K9 and Histone H3 Tri Methyl K4 as Prognostic Markers for Patients with Cervical Cancer

Beyer

Zhu

Mayr

et al. 2017

IJMS

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Chromatin remodeling alters gene expression in carcinoma tissue. Although cervical cancer is the fourth most common cancer in women worldwide, a systematic study about the prognostic value of specific changes in the chromatin structure, such as histone acetylation or histone methylation, is missing. In this study, the expression of histone H3 acetyl K9, which is known to denote active regions at enhancers and promoters, and histone H3 tri methyl K4, which preferentially identifies active gene promoters, were examined as both show high metastatic potential. A panel of patients with cervical cancer was selected and the importance of the histone modifications concerning survival-time (overall survival and relapse-free survival) was analyzed in 250 cases. Histone H3 acetyl K9 staining was correlated with low grading, low FIGO (TNM classification and the International Federation of Gynecology and Obstetrics) status, negative N-status and low T-status in cervical cancer, showing a higher expression in adenocarcinoma than in squamous cell carcinoma. Cytoplasmic expression of histone H3 tri methyl K4 in a cervical cancer specimen was correlated with advanced T-status and poor prognosis. While cytoplasmic H3K4me3 expression seemed to be a marker of relapse-free survival, nuclear expression showed a correlation to poor prognosis in overall survival. Within this study, we analyzed the chemical modification of two histone proteins that are connected to active gene expression. Histone H3 acetyl K9 was found to be an independent marker of overall survival. Histone H3 tri methyl K4 was correlated with poor prognosis and it was found to be an independent marker of relapse-free survival. Therefore, we could show that chromatin remodeling plays an important role in cervical cancer biology.

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Section: Discussionmentioning

confidence: 99%

Histone H3 Acetyl K9 and Histone H3 Tri Methyl K4 as Prognostic Markers for Patients with Cervical Cancer

Beyer

Zhu

Mayr

et al. 2017

IJMS

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“…[21,22] We used the same assay and found ac onsistentn ucleosome dissociation pattern through which H2A-H2B andH 3-H4 dissociated from DNA at around 75.5(AE 0.6) 8Ca nd 86.4(AE 0.7) 8C, respectively ( Figure 1C,T able S1). [21,22] We used the same assay and found ac onsistentn ucleosome dissociation pattern through which H2A-H2B andH 3-H4 dissociated from DNA at around 75.5(AE 0.6) 8Ca nd 86.4(AE 0.7) 8C, respectively ( Figure 1C,T able S1).…”

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confidence: 84%

Direct Observation of H3–H4 Octasome by High‐Speed AFM

Zou

Hashiya

Wei

et al. 2018

Chemistry A European J

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Despite evidence that histone H3 and H4 proteins may act as the precursor for orientating the DNA sequence to form nucleosome structures, there is no direct evidence of the formed compact structure. Here, it is demonstrated that a histone H3-H4 octasome could be constructed without the involvement of histone H2A-H2B under in vitro reconstitution conditions. Atomic force microscopy was used to obtain the first direct observation of the octasome structure, which exhibited a similar core-protein size as that of a nucleosome but with a shorter core histone-binding DNA region. The octasome also displayed a one-step histone-dissociation pattern under heat treatment, distinct micrococcal nuclease and peplomycin accessibility, which suggests a different wrapping pattern to that in nucleosomes.

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“…The crystal structure of the human nucleosome containing H3.1, H4, H2A type 1-B/E, and H2B type 1-J (PDB: 3W98) is shown. 45 The histones are colored according to the legend, with Asp/Glu residues that were found to be ADP-ribosylated shown in red spheres. Note that PDB structure does not contain full length histones and so not all identified sites are displayed in the figure (structure contains H3.1: AA 38–136, H4: 19–104, H2A type 1-B/E: 13–118, H2B type 1-J: 30–124).…”

Section: Figurementioning

confidence: 99%

The nucleosomal surface is the main target of histone ADP-ribosylation in response to DNA damage

et al. 2017

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ADP-ribosylation is a protein post-translational modification catalyzed by ADP-ribose transferases (ARTs). ART activity is critical in mediating many cellular processes, and is required for DNA damage repair. All five histone proteins are extensively ADP-ribosylated by ARTs upon induction of DNA damage. However, how these modifications aid in repair processes is largely unknown, primarily due to lack of knowledge about where they site-specifically occur on histones. Here, we conduct a comprehensive analysis of histone Asp/Glu ADP-ribosylation sites upon DNA damage induced by dimethyl sulfate (DMS). We also demonstrate that incubation of cell nuclei with NAD+, as has been done previously in the literature, leads to spurious ADP-ribosylation levels of histone proteins. Altogether, we were able to identify 30 modification sites, 20 of which are novel. We also quantify the abundance of these modification sites during the course of DNA damage insult to identify which sites are critical for mediating repair. We found that every quantifiable site increases in abundance over time and that each identified ADP-ribosylation site is located on the surface of the nucleosome. Together, the data suggest specific Asp/Glu residues are unlikely to be critical for DNA damage repair and rather that this process is likely dependent on ADP-ribosylation of the nucleosomal surface in general.

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Contribution of histone N‐terminal tails to the structure and stability of nucleosomes

Cited by 118 publications

References 53 publications

Histone H3 Acetyl K9 and Histone H3 Tri Methyl K4 as Prognostic Markers for Patients with Cervical Cancer

Histone H3 Acetyl K9 and Histone H3 Tri Methyl K4 as Prognostic Markers for Patients with Cervical Cancer

Direct Observation of H3–H4 Octasome by High‐Speed AFM

The nucleosomal surface is the main target of histone ADP-ribosylation in response to DNA damage

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