Immunological evidence for an H1° type of histone protein in chicken liver

Moorman, Antoon F.M.; Boer, Piet A. J. de; Smit-Vis, J.H.; Lamers, Wouter H.; Charles, Roger

doi:10.1111/j.1432-0436.1986.tb00554.x

Cited by 15 publications

(9 citation statements)

References 27 publications

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“…Their preparation and specificity, as determined by Western-blot analysis, have been described elsewhere [20]. Their preparation and specificity, as determined by Western-blot analysis, have been described elsewhere [20].…”

Section: Antibodiesmentioning

confidence: 99%

Immunohistochemical analysis of the distribution of histone H5 and hemoglobin during chicken development

et al. 1987

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Section: Antibodiesmentioning

confidence: 99%

Immunohistochemical analysis of the distribution of histone H5 and hemoglobin during chicken development

et al. 1987

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“…cells in the brain, retina, striated muscle, cardiac muscle and liver (Gjerset et al, 1982). Histone H1" (or related uncharacterized members of the family) is found in all vertebrates examined, including fishes (Miki and Neelin, 1975), reptiles (Rutledge et al, 1981) and birds (Moorman et al, 1986;Srebreva et al, 1983). In amphibians there is a confusion regarding identity of H1.…”

Section: Differentiation-specific Histone Hi (Hi O H5)mentioning

confidence: 99%

“…The H1" promoter contains a histone-specific H1 box (Figs 3 and 4A), whereas the H5 promoter incorporates several erythroid-specific elements and has become a tissue-specific gene. Although the H1" gene has not yet been cloned in birds, the protein has been observed (Moorman et a]., 1986;Srebreva et al, 1983). In mammals, the H5 gene is no longer present and H1" represents the only differentiation-specific linker histone (Alonso et al, 1988).…”

Section: Gene Structures Of Linker-histone Variantsmentioning

confidence: 99%

Developmentally regulated expression of linker‐histone variants in vertebrates

Khochbin

Wolffe

1994

European Journal of Biochemistry

101

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The identification of histone H1 variants in vertebrates suggests that these proteins may have specialized functions. During embryonic development, a correspondence between the expression of each of the linker-histone variants and the proliferative and transcriptional activity of embryonic cells can be observed. Analysis of the developmentally regulated expression of these variants leads to the subdivision of these variants into distinct classes. This subdivision may also provide insight into the significance of the differential expression of variants and the roles individual linker histones have in chromatin structure and function.Linker histones have long been known to interact with the variable length of linker DNA that lies between nucleosome cores within chromatin (van Holde, 1989). This interaction is believed to facilitate the folding of nucleosomal arrays into higher-order structures. This mundane packaging role is, not, however, the only role linker histones have to play. Studies on the structure of linker histones, their interaction with the nucleosome and their roles in controlling gene activity indicate that this family of proteins has not only an important architectural role, but also an essential regulatory role in transcription. In vertebrates, several different variants of linker histones have been described and the expression of their genes studied. It is useful to examine the properties and expression of these variants, since this analysis leads to a better understanding of the relevance of this diversity for particular cellular activities during development.Linker histones may be subdivided into four major classes according to both the timing of their expression and their cell-type specificity during development. This division, based on the pattern of expression, corresponds also to distinct properties of proteins in each class. In general, a linker histone presents a tripartite structure; an N-terminal tail, a globular domain and a relatively long C-terminal tail. Members of each class have conserved this structural feature but can ble distinguished mainly by the length of the N-terminal and C-terminal tails and the nature of the peptide sequence, i.e. the number of acidic and basic amino acids as well as the nature of the basic residues.Cleavage linker histones are expressed during oogenesis and during early embryogenesis. The normal somatic form of linker histone (Hl) progressively accumulates in nuclei after the initiation of zygotic expression and, thereafter, is Correspondence to S. Khochbin,

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“…However, this supposed role is mainly based on in vitro observations and has not been verified by detailed analyses of the way in which this protein appears during embryonic development in vivo. Histone H5 represents the erythrocyte-specific variant in birds [14,151. This variant seems involved in thc establishment and maintenance of the highly repressed statc of the erythrocyte chromatin [5].…”

Section: Introductionmentioning

confidence: 85%

“…Lysine-rich histones were prepared from tadpole homogenates in 0.14 A4 NaCl by extraction with 5% (w/v) perchloric acid [14]. Adult erythrocytes were first washed in amphibian phosphate-buffered saline and lysed in distilled water, and then lysine-rich histone were extracted with 5% (w/v) perchloric acid.…”

Section: Isolation and Analysis Of Histonesmentioning

confidence: 99%