Non-allelic variants of histones 2a, 2b and 3 in mammals

Franklin, Samuel G.; Zweidler, Alfred

doi:10.1038/266273a0

Cited by 302 publications

(150 citation statements)

References 19 publications

Supporting

Mentioning

142

Contrasting

Unclassified

Order By: Relevance

“…Three human variants of H3 have been reported including H3.1, H3.2, and H3.3. H3.1 and H3.2 differ by one amino acid residue (H3.1 C96 vs H3.2 S96) and are deposited onto DNA during S-phase [42]. H3.3 differs from H3.1 by five substitutions (A31S, S87A, V89I, M90G and C96S) [43,44].…”

Section: Core Histone Profilesmentioning

confidence: 99%

“…(14,032 Da) could only possibly be present in gel band 1 as no peptide containing S40 was observed in gel band 0 and 2. The only possible sequence that contained G37N38, A40 ( 36 KGNYAER 42 . This modification could occur on H2AFC/D/I/N/P, H2AFL, H2AFE and/or H2AFS due to the sequence homology for fragment 89−99.…”

Section: Characterization Of Differential Expressed Histone Form As Dmentioning

confidence: 99%

See 1 more Smart Citation

Liquid chromatography mass spectrometry profiling of histones

Jacob

Amunugama

et al. 2007

Journal of Chromatography B

View full text Add to dashboard Cite

Here we describe the use of reverse-phase liquid chromatography mass spectrometry (RP-LC-MS) to simultaneously characterize variants and post-translationally modified isoforms for each histone. The analysis of intact proteins significantly reduces the time of sample preparation and simplifies data interpretation. LC-MS analysis and peptide mass mapping have previously been applied to identify histone proteins and to characterize their post-translational modifications. However, these studies provided limited characterization of both linker histones and core histones. The current LC-MS analysis allows for the simultaneous observation of all histone PTMs and variants (both replacement and bulk histones) without further enrichment, which will be valuable in comparative studies. Protein identities were verified by the analysis of histone H2A species using RPLC fractionation, AU-PAGE separation and nano-LC-MS/MS.

show abstract

Section: Core Histone Profilesmentioning

confidence: 99%

Section: Characterization Of Differential Expressed Histone Form As Dmentioning

confidence: 99%

Liquid chromatography mass spectrometry profiling of histones

Jacob

Amunugama

et al. 2007

Journal of Chromatography B

View full text Add to dashboard Cite

show abstract

“…It should be noted that the predominant variant, referred to here as H3, in mammals consists of two subtypes: H3.1 and H3.2, which differ only at amino acid 96 (cysteine vs. serine) (Franklin and Zweidler 1977). In .…”

Section: Ncps Containing Untagged H33 Are Also Unstablementioning

confidence: 99%

Nucleosome stability mediated by histone variants H3.3 and H2A.Z

Jin

Felsenfeld²

2007

Genes Dev.

500

462

View full text Add to dashboard Cite

Nucleosomes containing the histone variant H3.3 tend to be clustered in vivo in the neighborhood of transcriptionally active genes and over regulatory elements. It has not been clear, however, whether H3.3-containing nucleosomes possess unique properties that would affect transcription. We report here that H3.3 nucleosomes isolated from vertebrates, regardless of whether they are partnered with H2A or H2A.Z, are unusually sensitive to salt-dependent disruption, losing H2A/H2B or H2A.Z/H2B dimers. Immunoprecipitation studies of nucleosome core particles (NCPs) show that NCPs that contain both H3.3 and H2A.Z are even less stable than NCPs containing H3.3 and H2A. Intriguingly, NCPs containing H3 and H2A.Z are at least as stable as H3/H2A NCPs. These results establish an hierarchy of stabilities for native nucleosomes carrying different complements of variants, and suggest how H2A.Z could play different roles depending on its partners within the NCP. They also are consistent with the idea that H3.3 plays an active role in maintaining accessible chromatin structures in enhancer regions and transcribed regions. Consistent with this idea, promoters and enhancers at transcriptionally active genes and coding regions at highly expressed genes have nucleosomes that simultaneously carry both H3.3 and H2A.Z, and should therefore be extremely sensitive to disruption.

show abstract

“…Histones comprise the principal protein component of chromatin and are involved in the regulation of gene expression (3,4). This epigenetic regulation is achieved through complex patterns of post-translational modifications (PTMs), 1 the incorporation of histone variants, and through controlled histone proteolysis (5)(6)(7)(8)(9)(10). Comprehensive characterization of histones by mass spectrometry (MS) has proven technically difficult for a number of reasons.…”

mentioning

confidence: 99%

Analyses of Histone Proteoforms Using Front-end Electron Transfer Dissociation-enabled Orbitrap Instruments

Anderson

Karch

Ugrin

et al. 2016

Molecular & Cellular Proteomics

View full text Add to dashboard Cite

Chromatin is the structural framework that packages DNA into chromosomes within the nucleus of a cell (2). Histones comprise the principal protein component of chromatin and are involved in the regulation of gene expression (3,4). This epigenetic regulation is achieved through complex patterns of post-translational modifications (PTMs), 1 the incorporation of histone variants, and through controlled histone proteolysis (5-10). Comprehensive characterization of histones by mass spectrometry (MS) has proven technically difficult for a number of reasons. Traditional methods (bottom-up MS) of sequence determination and PTM site localization are not practical. Histone N-terminal regions are rich in lysine and arginine residues, and thus proteolysis using trypsin generates peptides that are too small or that are poorly retained on reversephase HPLC C18 resins for subsequent MS detection (11). With the advent of electron transfer dissociation (ETD) and more efficient electron capture dissociation fragmentation methods, which are better suited for larger, more highly charged peptides (12, 13), several studies utilizing other endoproteases to generate longer peptides have emerged (14 -16). Although these methodologies do well to preserve the combinatorial PTM profiles of histone tails, in some cases it is still impossible to identify the proteoforms from which these peptides originate. This is why analyzing histones intact, as they exist in the cells from which they are derived, is the best method for identifying unique histone proteoforms.The results of several recent studies involving top-down analyses of histones highlight the complexity of the histone From the ‡Department

show abstract

Non-allelic variants of histones 2a, 2b and 3 in mammals

Cited by 302 publications

References 19 publications

Liquid chromatography mass spectrometry profiling of histones

Liquid chromatography mass spectrometry profiling of histones

Nucleosome stability mediated by histone variants H3.3 and H2A.Z

Analyses of Histone Proteoforms Using Front-end Electron Transfer Dissociation-enabled Orbitrap Instruments

Contact Info

Product

Resources

About