Histone Acetylation in Insect Chromosomes

Allfrey, Vincent G.; Pogo, Beatríz G. T.; Littau, Virginia C.; Gershey, Edward L.; Mirsky, A. E.

doi:10.1126/science.159.3812.314

Cited by 85 publications

(41 citation statements)

References 12 publications

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“…Histone H4 can be acetylated at several lysine residues (K5, K8, K12 and K16) on its N-terminal tail in all eukaryotes (Allfrey et al, 1968). K16 acetylation is the most abundant of these modifications in human cells (Munks et al, 1991).…”

Section: H4k16ac In Chromatin Organizationmentioning

confidence: 99%

Males absent on the first (MOF): from flies to humans

2007

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Histone modifications such as acetylation, methylation and phosphorylation have been implicated in fundamental cellular processes such as epigenetic regulation of gene expression, organization of chromatin structure, chromosome segregation, DNA replication and DNA repair. Males absent on the first (MOF) is responsible for acetylating histone H4 at lysine 16 (H4K16) and is a key component of the MSL complex required for dosage compensation in Drosophila. The human ortholog of MOF (hMOF) has the same substrate specificity and recent purification of the human and Drosophila MOF complexes showed that these complexes were also highly conserved through evolution. Several studies have shown that loss of hMOF in mammalian cells leads to a number of different phenotypes; a G 2 /M cell cycle arrest, nuclear morphological defects, spontaneous chromosomal aberrations, reduced transcription of certain genes and an impaired DNA repair response upon ionizing irradiation. Moreover, hMOF is involved in ATM activation in response to DNA damage and acetylation of p53 by hMOF influences the cell's decision to undergo apoptosis instead of a cell cycle arrest. These data, highlighting hMOF as an important component of many cellular processes, as well as links between hMOF and cancer will be discussed.

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Section: H4k16ac In Chromatin Organizationmentioning

confidence: 99%

Males absent on the first (MOF): from flies to humans

2007

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“…Histone migration and proteolysis were minimized by using low ionic strength media and by including sodium bisulfite. Nuclei were prepared from calf thymus essentially following Allfrey et al (18) with the inclusion of 10 mM sodium bisulfite, and purified through 2.4 M sucrose. Minimally sheared chromatin, in the gel state, was prepared by hypotonic shock of the purified nuclei (19 (20).…”

Section: Methodsmentioning

confidence: 99%

Chromatin architecture: investigation of a subunit of chromatin by dark field electron microscopy.

Langmore¹,

Wooley²

1975

Proc. Natl. Acad. Sci. U.S.A.

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Dark field scanning electron microscopy of unstained, unfixed samples of chromatin, histone-l-depleted chromatin, and nucleohistone has been used to identify an apparent subunit of chromatin, namely a disk-shaped structure we term the unit particle, which is probably about 135 A wide and 50 A thick in the hydrated state. The unit particles are found at rather uniform intervals along thin DNA-like fibers. Histone 1 depletion leads to a bimodal distribution of these spacings. Our observations suggest that the unit particle consists of a loop of nucleoprotein, perhaps around a histone core.After many attempts, with limited success, to describe the structure of the eukaryotic genetic material as a continuous structure, investigators are now turning their attention to models of a more discontinuous structure, involving subunits which might be "assembled" into chromatin. (20).The chemical composition and stoichiometry of the samples were characterized using the procedures of Bonner et al. (20). Intact chromatin possessed a total histone/DNA weight ratio of 1.12 I 0.04, an H1/DNA ratio of 0.29 + 0.02, and a non-histone protein/DNA ratio of 0.55 I 0.03. The histone/DNA ratio of HI-depleted chromatin was 0.83 + 0.02; no non-histone proteins were found. The nucleohistone had a ratio of histone/DNA of 1.02 I 0.02 and an Hi/ DNA ratio of 0.14 + 0.02; no non-histone proteins were found.All specimen solutions were "desalted" immediately before preparation, by exclusion on Sephadex G-100 equilibrated with 1 mM NaPO4, pH 7.0. About 2 gl of this Mg/ml solution of chromatin were then placed on a 20-30 A thick hydrophilic carbon film, blotted, and air dried.Electron Microscopy. All specimens were examined at 30 keV in dark field using the high-resolution scanning transmission electron microscope developed in the laboratory of . Microscope operating conditions were as described before, except that we chose not to outgas the specimen by baking (17). The elastically and inelastically scattered electron signals were usually simultaneously stored in digital form directly on magnetic tape, using a 512 X 512 picture element format (16,17). At low instrumental magnification each picture element represented 15.4 A at the specimen; at high magnification each picture element represented 4.96 A. The magnification was determined from

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“…Although the secondary modification of histones by acetylation of lysine N 6 -amino groups ( Fig. 1) has been known for 40 years (12,13), it has only recently been identified as a critical determinant of gene expression (14) and a general modulator of p53 and other transcription factors (15,16). Unlike the N-terminal ␣-acetylation of proteins that occurs with translation, lysine N 6 -acetylation is reversible and occurs at highly conserved sites in the N-terminal tails of histone proteins (14).…”

mentioning

confidence: 99%

N-formylation of lysine in histone proteins as a secondary modification arising from oxidative DNA damage

Jiang

Zhou

Taghizadeh

et al. 2007

Proc. Natl. Acad. Sci. U.S.A.

188

200

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The posttranslational modification of histone and other chromatin proteins has a well recognized but poorly defined role in the physiology of gene expression. With implications for interfering with these epigenetic mechanisms, we now report the existence of a relatively abundant secondary modification of chromatin proteins, the N 6 -formylation of lysine that appears to be uniquely associated with histone and other nuclear proteins. Using both radiolabeling and sensitive bioanalytical methods, we demonstrate that the formyl moiety of 3 -formylphosphate residues arising from 5 -oxidation of deoxyribose in DNA, caused by the enediyne neocarzinostatin, for example, acylate the N 6 -amino groups of lysine side chains. A liquid chromatography (LC)-tandem mass spectrometry (MS) method was developed to quantify the resulting N 6 -formyl-lysine residues, which were observed to be present histone acetylation ͉ oxidative stress ͉ enediyne

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Histone Acetylation in Insect Chromosomes

Cited by 85 publications

References 12 publications

Males absent on the first (MOF): from flies to humans

Males absent on the first (MOF): from flies to humans

Chromatin architecture: investigation of a subunit of chromatin by dark field electron microscopy.

N-formylation of lysine in histone proteins as a secondary modification arising from oxidative DNA damage

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