Hypophysotropic activity of histone H3 in vitro
To assess the effect of histone H3 on pituitary hormone secretion, rat anterior pituitary (AP) cells were used and growth hormone, prolactin, thyrotropin, luteinizing hormone and follicle stimulating hormone measured by radioimmunoassay. Incubation of cells with H3 (1, 6, and 30 microM) stimulated the release of all five hormones in a dose-dependent ...
Brown, Oscar Alfredo+4 more
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Histone H3 phosphorylation and cell division [PDF]
Histone H3 is specifically phosphorylated during both mitosis and meiosis in patterns that are specifically coordinated in both space and time. Histone H3 phosphorylation may initiate at different phases of the cell division in different organisms, but metaphase chromosomes are always found to be heavily phosphorylated.
Fabienne Hans, Stefan Dimitrov
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The histone chaperone Vps75 forms multiple oligomeric assemblies capable of mediating exchange between histone H3–H4 tetramers and Asf1–H3–H4 complexes [PDF]
Wellcome Trust [094090, 097945, 099149]; Medical Research Council [G1100021]. Funding for open access charge: Wellcome Trust.Vps75 is a histone chaperone that has been historically characterized as homodimer by X-ray crystallography.
Angus Lamond+11 more
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DNA mismatch repair interacts with CAF-1- and ASF1A-H3-H4-dependent histone (H3-H4)2 tetramer deposition. [PDF]
DNA mismatch repair (MMR) is required for the maintenance of genome stability and protection of humans from several types of cancer. Human MMR occurs in the chromatin environment, but little is known about the interactions between MMR and the chromatin ...
Kadyrov, Farid A+2 more
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NuA4 Links Methylation of Histone H3 Lysines 4 and 36 to Acetylation of Histones H4 and H3 [PDF]
Cotranscriptional methylation of histone H3 lysines 4 and 36 by Set1 and Set2, respectively, stimulates interaction between nucleosomes and histone deacetylase complexes to block cryptic transcription in budding yeast. We previously showed that loss of all H3K4 and H3K36 methylation in a set1Δset2Δ mutant reduces interaction between native nucleosomes ...
Bing Li+5 more
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Centromere Silencing and Function in Fission Yeast Is Governed by the Amino Terminus of Histone H3 [PDF]
Background: Centromeric domains often consist of repetitive elements that are assembled in specialized chromatin, characterized by hypoacetylation of histones H3 and H4 and methylation of lysine 9 of histone H3 (K9-MeH3).
Allshire, Robin C.+5 more
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Investigation of in vitro histone H3 glycosylation using H3 tail peptides
AbstractPosttranslational modifications (PTMs) on histone tails regulate eukaryotic gene expression by impacting the chromatin structure and by modulating interactions with other cellular proteins. One such PTM has been identified as serine and threonine glycosylation, the introduction of the ß-N-acetylglucosamine (GlcNAc) moiety on histone H3 tail at ...
Merx, Jona+10 more
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Histone Mutants Separate R Loop Formation from Genome Instability Induction [PDF]
R loops have positive physiological roles, but they can also be deleterious by causing genome instability, and the mechanisms for this are unknown. Here we identified yeast histone H3 and H4 mutations that facilitate R loops but do not cause instability.
Aguilera López, Andrés+5 more
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Extended Recognition of the Histone H3 Tail by Histone Demethylase KDM5A [PDF]
ABSTRACTHuman lysine demethylase KDM5A is a chromatin modifying enzyme associated with transcriptional regulation due to its ability to catalyze removal of methyl groups from methylated lysine 4 of histone H3 (H3K4me3). Amplification of KDM5A is observed in a number of cancers, including breast cancer, prostate cancer, hepatocellular carcinoma, lung ...
Petronikolou, Nektaria+2 more
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Structural insight into how the human helicase subunit MCM2 may act as a histone chaperone together with ASF1 at the replication fork [PDF]
International audienceMCM2 is a subunit of the replicative helicase machinery shown to interact with histones H3 and H4 during the replication process through its N-terminal domain.
Almouzni, Geneviève+13 more
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