Characterisation of human histone H1x

Happel, Nicole; Schulze, Ekkehard; Doenecke, Detlef

doi:10.1515/bc.2005.064

Cited by 58 publications

(73 citation statements)

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“…S1). H1x is an H1-variant that appears to be present in chromatin inaccessible to micrococcal nuclease, although very little is known about it (35). We also identified the spermspecific basic protein 4, as determined by mass spectrometry of the gel slices.…”

Section: Resultsmentioning

confidence: 98%

Analysis of Histones in Xenopus laevis

Shechter

Nicklay

Chitta

et al. 2009

Journal of Biological Chemistry

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Histone proteins contain epigenetic information that is encoded both in the relative abundance of core histones and variants and particularly in the post-translational modification of these proteins. We determined the presence of such variants and covalent modifications in seven tissue types of the anuran Xenopus laevis, including oocyte, egg, sperm, early embryo equivalent (pronuclei incubated in egg extract), S3 neurula cells, A6 kidney cells, and erythrocytes. We first developed a new robust method for isolating the stored, predeposition histones from oocytes and eggs via chromatography on heparin-Sepharose, whereas we isolated chromatinized histones via conventional acid extraction. We identified two previously unknown H1 isoforms (H1fx and H1B.Sp) present on sperm chromatin. . Furthermore, we subjected a subset of these histones to two-dimensional gel analysis and subsequent immunoblotting and mass spectrometry to determine the global remodeling of histone modifications that occurs as development proceeds. Overall, our observations suggest that each metazoan cell type may have a unique histone modification signature correlated with its differentiation status.

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Section: Resultsmentioning

confidence: 98%

Analysis of Histones in Xenopus laevis

Shechter

Nicklay

Chitta

et al. 2009

Journal of Biological Chemistry

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“…The constitution and a possible age-dependent change of the various H1 subtypes was initially analysed by Western blotting using H1 subtype H1 histones for these subtypes, in two recent papers from our group (see Happel et al, 2005 andStoldt et al, 2007, respectively). Sulfuric acidextracted H1 histones from donors of four age-groups were separated by SDS-PAGE and transferred to nitrocellulose membranes (Fig.…”

Section: Analysis Of H1 Subtype Composition Of Pbl By Western Blottingmentioning

confidence: 99%

“…In mammals, there are five H1 somatic subtypes, H1.1, H1.2, H1.3, H1.4 and H1.5 (Eick, et al, 1989;Albig et al, 1991;1993;1996b;Drabent et al, 1995a, reviewed in Doenecke et al, 1997, the replacement H1 subtype, H1 o (Gjerset et al, 1981;1982), the ubiquitous H1x (Yamamoto and Horikoshi, 1996;Happel et al, 2005), the testis-specific subtypes, H1t, H1T2 and HILS1 (Meistrich et al, 1985;1994;Drabent et al, 1996;Martianov et al, 2005;Yan et al, 2003) and an oocyte-specific subtype (Tanaka et al, 2001). Moreover, classic in vitro investigations analyzed the role of this histone family in chromatin structure and function.…”

Section: Introductionmentioning

confidence: 99%

H1 histone subtype constitution and phosphorylation state of the ageing cell system of human peripheral blood lymphocytes

Happel

Doenecke

Sekeri‐Pataryas

et al. 2008

Experimental Gerontology

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“…There are few studies characterizing the most recently identified and distantly related human variant, H1X, and its specific function in the cell remains unknown. Like H1.0, it has been suggested that H1X is enriched in a less accessible region of chromatin, but expression of the two variants is regulated differently (7). It has been shown previously that H1X accumulates in nucleoli in G 1 and is distributed across the entire nucleus in the S phase (8).…”

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confidence: 99%

Genome Distribution of Replication-independent Histone H1 Variants Shows H1.0 Associated with Nucleolar Domains and H1X Associated with RNA Polymerase II-enriched Regions

Mayor¹,

Izquierdo‐Bouldstridge²,

Millán-Ariño³

et al. 2015

Journal of Biological Chemistry

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Background: There are seven histone H1 variants in somatic mammalian cells, two of which are replication-independent, H1.0 and H1X. Results: In breast cancer cells, H1.0 is enriched at nucleolus-associated domains, whereas H1X is associated with RNA polymerase II-enriched regions. Conclusion: Most H1 variants show great redundancy across the genome, but there is also some specificity. Significance: Some H1 variants may have specific functions.Unlike core histones, the linker histone H1 family is more evolutionarily diverse, and many organisms have multiple H1 variants or subtypes. In mammals, the H1 family includes seven somatic H1 variants; H1.1 to H1.5 are expressed in a replicationdependent manner, whereas H1.0 and H1X are replication-independent. Using ChIP-sequencing data and cell fractionation, we have compared the genomic distribution of H1.0 and H1X in human breast cancer cells, in which we previously observed differential distribution of H1.2 compared with the other subtypes. We have found H1.0 to be enriched at nucleolus-associated DNA repeats and chromatin domains, whereas H1X is associated with coding regions, RNA polymerase II-enriched regions, and hypomethylated CpG islands. Further, H1X accumulates within constitutive or included exons and retained introns and toward the 3 end of expressed genes. Inducible H1X knockdown does not affect cell proliferation but dysregulates a subset of genes related to cell movement and transport. In H1X-depleted cells, the promoters of up-regulated genes are not occupied specifically by this variant, have a lower than average H1 content, and, unexpectedly, do not form an H1 valley upon induction. We conclude that H1 variants are not distributed evenly across the genome and may participate with some specificity in chromatin domain organization or gene regulation.There are five major classes of histones that participate in the correct folding of eukaryotic DNA into chromatin: the core histones H2A, H2B, H3, and H4, which form an octamer and constitute the nucleosome core particle, and the linker histone H1, which binds to the nucleosomes near the entry/exit sites of linker DNA. Stabilization of the condensed states of chromatin is the function most commonly attributed to the linker histone (1, 2), in addition to its inhibitory effect in vitro on nucleosome mobility (3) and transcription (4).Histone H1 in humans is a family of closely related, single gene-encoded proteins, including seven somatic subtypes (H1.1 to H1.5, H1.0, and H1X), three testis-specific variants (H1t, H1T2, and HILS1), and one restricted to oocytes (H1oo) (5, 6). Among the somatic histone H1 variants, H1.1 to H1.5 are expressed in a replication-dependent manner, whereas H1.0 and H1X are replication-independent. The H1.1 to H1.5-encoding genes are clustered in a region of chromosome 6 together with the core histone genes, whereas the H1X and H1.0 genes are on chromosomes 3 and 22, respectively. H1.2 to H1.5 and H1X are ubiquitously expressed, H1.1 is restricted to certain tissues, and H1.0 accumulat...

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Characterisation of human histone H1x

Cited by 58 publications

References 58 publications

Analysis of Histones in Xenopus laevis

Analysis of Histones in Xenopus laevis

H1 histone subtype constitution and phosphorylation state of the ageing cell system of human peripheral blood lymphocytes

Genome Distribution of Replication-independent Histone H1 Variants Shows H1.0 Associated with Nucleolar Domains and H1X Associated with RNA Polymerase II-enriched Regions

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