Posttranslational modifications of human histone H3: An update

  title={Posttranslational modifications of human histone H3: An update},
  author={Yan-Ming Xu and Ji-Ying Du and Andy T. Y. Lau},
Histone proteins, the fundamental components of chromatin, are highly conserved proteins that present in eukaryotic nuclei. They organize genomic DNA to form nucleosomes, the basic units of chromatin. PTMs of histones play essential roles in many biological processes, such as chromatin condensation, gene expression, cell differentiation, and apoptosis. With the advancement of proteomic technology, a growing number of histone PTMs have been identified, including ADP‐ribosylation, biotinylation… 

Top-down characterization of mouse core histones.

This study presents a general picture of combinatorial PTMs of mouse core histones, which serves as a basic reference for all future related biological studies and allows the unambiguous identification of acetylation instead of trimethylation.

Modulation of nucleosomal DNA accessibility via charge-altering post-translational modifications in histone core

A physics-based framework is proposed that predicts the effect of charge-altering PTMs in the histone core, quantitatively for several types of lysine charge-neutralizing PTMs including acetylation, and qualitatively for all phosphorylations, on the nucleosome stability and subsequent changes in DNA accessibility, making a connection to resulting biological phenotypes.

Histone Post-Translational Modifications and Nucleosome Organisation in Transcriptional Regulation: Some Open Questions.

This review focuses on the presence of multiple histone post-translational modifications on a single nucleosome and the methods to detect them and their meaning, with special emphasis on bivalent marks.

Structural insights into the molecular mechanism underlying Sirt5-catalyzed desuccinylation of histone peptides.

It is demonstrated that human sirtuin 5 (Sirt5) catalyzes the sequence-selective desuccinylation of numerous histone succinyl sites, and structural studies of Sirt5 in complex with four succinyl peptides indicate an essential role for the conserved main chain hydrogen bonds formed by the succinyl lysine, +1, +3 sites for substrate-enzyme recognition.

Posttranslational modifications of CENP-A: marks of distinction

The posttranslational modification (PTM) of histone proteins is a major mechanism regulating the function of chromatin and the importance of these modifications in its deposition at centromeres, protein stability, and recruitment of the CCAN is uncovered.

Canonical and Variant Forms of Histone H3 Are Deposited onto the Human Cytomegalovirus Genome during Lytic and Latent Infections

Show that HCMV genomes are loaded with canonical and variant H3 histones during both lytic and latent infections strengthens the hypothesis that chromatinization pathways are similar between the two infection types, implicates virion or cellular factors in this process, and exposes the possibility that histone variants, in addition to posttranslational modification, may impact viral gene expression.

Phosphorylation of Drosophila CENP-A on serine 20 regulates protein turn-over and centromere-specific loading

It is shown that CENP-A is phosphorylated at serine 20 (S20) by casein kinase II and that in mitotic cells, theosphorylated form is enriched on chromatin and that S20 phosphorylation regulates the turn-over of prenucleosomal CENA by the SCFPpa-proteasome pathway.

O-linked β-N-acetylglucosamine modification and its biological functions

The recent advances on O-GlcNAc modification and its biological functions in animals and plants are summarized, and prospect of more special functions of O- GloverNAc will be revealed in plants is revealed.



Initial characterization of histone H3 serine 10 O-acetylation

The investigations reveal that histone H3 serine 10 acetylation (H3S10ac) is potentially linked to cell cycle progression and cellular pluripotency, and a glimpse into the functional implications of this H3-specific histone mark is provided.

Inducible Covalent Posttranslational Modification of Histone H3

This STKE Review focuses mainly on the inducible phosphorylation of histone H3 brought about by different stimuli and examines the most recent research data concerning the identity of the hist one H3 kinases responsible for this phosphorylations.

Histone acetyltransferases.

This review discusses the current understanding of histone acetyl transferases (HATs) or acetyltransferases (ATs): their discovery, substrate specificity, catalytic mechanism, regulation, and functional links to transcription, as well as to other chromatin-modifying activities.

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

The N6-formyl modification of lysine may interfere with the signaling functions of l Lysine acetylation and methylation and thus contribute to the pathophysiology of oxidative and nitrosative stress.

A Peek into the Complex Realm of Histone Phosphorylation

ABSTRACT Although discovered long ago, posttranslational phosphorylation of histones has been in the spotlight only recently. Information is accumulating almost daily on phosphorylation of histones

Modifications of human histone H3 variants during mitosis.

When used together, mass spectrometry and immunoassay methods provide a powerful approach for elucidation of the histone code and identification of histone post-translational modifications that occur during mitosis and other specific cellular events.

Organismal Differences in Post-translational Modifications in Histones H3 and H4*

It is suggested that some post-translational modifications of histones are more conserved than previously thought, including H3K9me1 and H4K20me2 in yeast and H2K27me1, -me2, and -me3 in Tet.

Identification and verification of lysine propionylation and butyrylation in yeast core histones using PTMap software.

A systematic analysis of yeast histone PTMs by mass spectrometry in combination with protein sequence alignment using PTMap, a computer program recently developed, identifies multiple sites of lysine propionylation and butyrylation in yeast histones for the first time.