Characterization of a set of antibodies specific for three human histone H1 subtypes

Parseghian, Missag H.; Harris, Debra A.; Rishwain, Darron R.; Hamkalo, Barbara A.

doi:10.1007/bf00368013

Cited by 30 publications

(20 citation statements)

References 54 publications

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“…B Input samples (25 µg of HindIII/EcoRI-digested DNA-protein adducts) were treated with anti-RAP1 (lanes 1), anti-RNA polymerase II (lanes 2), a mixture of the three affinity-purified anti-linker histone IgGs (lanes 3) and probed with the sequences indicated below the panels gests that each of the common somatic H1s in mammals has distinct functions as has been argued on the basis of their evolutionary history (Ponte et al 1998). However, Parseghian et al (1993Parseghian et al ( , 1994 were unable to obtain an antibody against histone H1a and therefore were unable to localize all the human H1 variants. The localization pattern that we find in Arabidopsis is most similar to that of the midge (C. thummi) histones H1-II and -III, rat H1A and H1-B and human H1-1.…”

Section: Discussionmentioning

confidence: 96%

“…A similar set of results have been found in human cells, with H1A and H1-B binding throughout nuclei and H1°being restricted, being most abundant in nucleoli. The specific binding of the common H1 variants of human was investigated by Parseghian et al (1993Parseghian et al ( , 1994. They found that H1-1 (H1d) is uniformly distributed throughout nuclei, H1-2 and H1-4 (c and b) stain in a punctate pattern, and H1-3 (H1a) preferentially labels the nuclear periphery.…”

Section: Discussionmentioning

confidence: 99%

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Subnuclear distribution of the entire complement of linker histone variants in Arabidopsis thaliana

Ascenzi

Gantt

1999

Chromosoma

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Linker histones (e.g. H1, H5, H1 degrees ) are thought to exert control on chromatin function by restricting nucleosomal dynamics. All higher eukaryotes possess a diverse family of linker histones, which may exhibit functional specialization. Arabidopsis thaliana apparently contains a minimal complement of linker histone structural variants and therefore is an ideal model for investigating functional differentiation among linker histones. Histones H1-1 and H1-2 are relatively similar proteins that are expressed in a wide variety of tissues and make up the majority of linker histone while H1-3 is a highly divergent minor variant protein that is induced by drought stress. We are interested in determining whether the in vivo distribution of each of these proteins also differs. To this end, we have produced subtype-specific antibodies and have localized each of the three proteins at the intranuclear and DNA sequence levels by indirect immunofluorescence and immunoprecipitation, respectively. Antibodies against linker histones H1-1 and H1-2 decorate nuclei in patterns very similar to 4',6-diamidino-2-phenylindole (DAPI) staining, but different than the staining pattern of total histones. In contrast, antibodies made against two regions of H1-3 bind to chromatin in a diffuse pattern distinct from the DAPI-staining pattern. We also describe a technique to determine the localization of plant linker histone variants along regions of chromatin, employing in vivo chemical DNA-protein cross-linking to preserve native associations followed by immunoprecipitation with subtype-specific antibodies. We use this technique to demonstrate that, in contrast to the major linker histones, H1-3 does not bind the repetitive sequences pAL1 and 5S rDNA. In addition, we show that linker histones are bound to the compacted nucleosomal arrays at the telomere but with reduced stoichiometry. Taken together, our results suggest that plants, as has been shown for animals, possess a variant linker histone that is differentially localized.

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Section: Discussionmentioning

confidence: 96%

Section: Discussionmentioning

confidence: 99%

Subnuclear distribution of the entire complement of linker histone variants in Arabidopsis thaliana

Ascenzi

Gantt

1999

Chromosoma

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“…H1.4 and H1.5, suggests that additional kinases, not sensitive to these compounds, are acting on the isoforms. Distribution of the H1 isoforms to distinct regions of the nucleus may also contribute to the differential functionality of the isoforms (41,42) and such trafficking may depend on post-translational modifications of the proteins in response to varied stimuli (43,44). Future experiments will need to expand on the concept of individual histone H1 isoforms acting as gene-specific regulators of transcriptional activity through the modulation of chromatin structure.…”

Section: Discussionmentioning

confidence: 99%

Hormone-mediated Dephosphorylation of Specific Histone H1 Isoforms

Banks¹,

Deterding

Tomer

et al. 2001

Journal of Biological Chemistry

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We have previously shown a connection between histone H1 phosphorylation and the transcriptional competence of the hormone inducible mouse mammary tumor virus (MMTV) promoter. Prolonged exposure of mouse cells to dexamethasone concurrently dephosphorylated histone H1 and rendered the MMTV promoter refractory to hormonal stimulation and, therefore, transcriptionally unresponsive. Using electrospray mass spectrometry, we demonstrate here that prolonged dexamethasone treatment differentially effects a subset of the six somatic H1 isoforms in mouse cells. H1 isoforms H1.0, H1.1, and H1.2 are non-responsive to hormone whereas prolonged dexamethasone treatment effectively dephosphorylated the H1.3, H1.4, and H1.5 isoforms. The protein kinase inhibitor staurosporine, shown to dephosphorylate histone H1 and down-regulate MMTV in cultured cells, appears only to completely dephosphorylate the H1.3 isoform. These results suggest that dephosphorylation of specific histone H1 isoforms may contribute to the previously observed decrease in transcriptional competence of the MMTV promoter through the modulation of chromatin structure. In a broader sense, this work advances the hypothesis that post-translational modifications of individual histone H1 isoforms directly influence the transcriptional activation/repression of specific genes.Eukaryotic DNA is efficiently organized into the highly ordered yet dynamic structure called chromatin (1, 2). The primary, repeating structural unit of chromatin is the nucleosome and is composed of 146 base pairs of DNA wrapped around an octamer of four core histone proteins: H2A, H2B, H3, and H4 (3). In addition, the linker histone or histone H1 protein binds to the linker DNA between nucleosomes and is thought to function primarily in the condensation of chromatin into higher ordered structures (4). While the core histones are highly conserved in eukaryotes, with H4 being nearly invariant, histone H1 is much more evolutionarily diverse, and in mammals, consists of six somatic H1 isoforms (H1.0 through H1.5, using the nomenclature of Doenecke and co-workers, Ref. 5) and one testis-specific isoform (H1.t). The H1 isoforms share a common protein structural fold with the N-and C-terminal "tail" regions extending from a central globular domain. The central globular domain is primarily responsible for binding to DNA, while the tail regions function to modulate protein interaction with DNA (4). It is generally accepted that histone H1 binds nucleosomes at the dyad axis and contacts duplex DNA as it enters and exits the nucleosome (6). However, in the specific case of the 5 S rRNA gene from Xenopus, there is evidence to suggest that histone H1 binds asymmetrically to the nucleosome on a position off the dyad axis and within a DNA gyre (6 -8).A growing body of evidence suggests that the linker histones function in part to modulate transcriptional activity through chromatin organization (reviewed in Ref. 9). Initially, it was thought that histone H1 would have a general role in global gene activity, as ...

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“…Several different nomenclatures have been proposed: mH1.1-5 and hH1.1-5 (Drabent et al, 1995a;Albig et al, 1991), mouse H1a-H1e (Lennox & Cohen, 1983), human H1a-H1e (Ohe et al, 1989), the human and mouse H1 s -1 to H1 s -4 and H1a (Parseghian et al, 1994a), and the mouse H1var1 to H1var3 (Dong et al, 1994;Yang et al, 1987). The accession numbers for the sequences are given.…”

Section: Expression Of the Five Histone H1 Genesmentioning

confidence: 97%