Histones in functional diversification

Pusarla, Rama-Haritha; Bhargava, Poonam

doi:10.1111/j.1742-4658.2005.04930.x

Cited by 66 publications

(47 citation statements)

References 143 publications

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“…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]. These amino acid substitutions introduce changes in hydrophobicity of the H3 variants resulting in different retention times when separated by reverse-phase chromatography.…”

Section: Core Histone Profilesmentioning

confidence: 99%

Liquid chromatography mass spectrometry profiling of histones

Jacob

Amunugama

et al. 2007

Journal of Chromatography B

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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.

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Section: Core Histone Profilesmentioning

confidence: 99%

Liquid chromatography mass spectrometry profiling of histones

Jacob

Amunugama

et al. 2007

Journal of Chromatography B

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“…Histone variants are associated with changes in gene expression, DNA repair, meiosis and apoptosis [118]. Besides the aforementioned H2AX variant, the linker histone variant, H1.2, is also a marker of DNA damage-induced apoptosis.…”

Section: Changes In Chromatin Structure Associated With Other Stressesmentioning

confidence: 99%

Hypoxia-induced and stress-specific changes in chromatin structure and function

Johnson

Barton

2007

Mutation Research/Fundamental and Molecular Mechanisms of Mutag

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Cellular adaptation to stress relies on specific, regulated responses to evoke changes in gene expression. Stresses such as hypoxia, heat shock, oxidative stress and DNA-damage activate signaling cascades that ultimately lead to either induction or repression of stress-responsive genes. In this review, we concentrate on the mechanisms by which stress-induced signaling promotes alterations in chromatin structure, whether the read-out is activation or repression of transcription. Specific alterations in chromatin are highly regulated and dictated by the type of imposed stress. Our primary focus is on the types of chromatin alterations that occur under hypoxic conditions, which exist within a majority of tumors, and to compare these to changes in chromatin structure that occur in response to a wide variety of cellular stresses.

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“…9). Histone genes encoding these variants can be classified into three main subtypes on the basis of their expression pattern and genomic organization (10,11): replication-dependent (RD), replication-and cell cycle phaseindependent (RI), and tissue-specific (TS) histones.…”

Section: Histone H3 Variants and Their Evolutionmentioning

confidence: 99%

Histone H3 variants and their potential role in indexing mammalian genomes: The “H3 barcode hypothesis”

Hake

Allis

2006

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

389

315

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In the history of science, provocative but, at times, controversial ideas have been put forward to explain basic problems that confront and intrigue the scientific community. These hypotheses, although often not correct in every detail, lead to increased discussion that ultimately guides experimental tests of the principal concepts and produce valuable insights into long-standing questions. Here, we present a hypothesis, the ''H3 barcode hypothesis.'' Hopefully, our ideas will evoke critical discussion and new experimental approaches that bear on general topics, such as nuclear architecture, epigenetic memory, and cell-fate choice. Our hypothesis rests on the central concept that mammalian histone H3 variants (H3.1, H3.2, and H3.3), although remarkably similar in amino acid sequence, exhibit distinct posttranslational ''signatures'' that create different chromosomal domains or territories, which, in turn, influence epigenetic states during cellular differentiation and development. Although we restrict our comments to H3 variants in mammals, we expect that the more general concepts presented here will apply to other histone variant families in organisms that employ them.histone H3 variants H3.1, H3.2, H3.3 ͉ ''barcode hypothesis'' ͉ epigenetic memory ͉ cell differentiation

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Histones in functional diversification

Cited by 66 publications

References 143 publications

Liquid chromatography mass spectrometry profiling of histones

Liquid chromatography mass spectrometry profiling of histones

Hypoxia-induced and stress-specific changes in chromatin structure and function

Histone H3 variants and their potential role in indexing mammalian genomes: The “H3 barcode hypothesis”

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