Immunofluorescent localization of histone H10 in the nuclei of proliferating and differentiating friend cells

Banchev, Todor; Srebreva, Ljuba; Zlatanova, Jordanka; Tsanev, Roumen

doi:10.1016/0014-4827(88)90019-5

Cited by 31 publications

(12 citation statements)

References 20 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The stored histone could be used later, supplying the active chromatin close to the nucleoli (Tomanek et al, 1986(Tomanek et al, , 1988 (Tomanek et al, 1986), provided they are close to H1 units (Banchev et al, 1988), are only one of these nucleoproteins. We have demonstrated in this study that as soon as they appeared in nuclei, they were associated with, or determined the appearance of heterochromatin, probably in core particle units, while the rest of the chromatin was mostly unlabelled.…”

Section: Discussionmentioning

confidence: 99%

“…Successive nucleosomes are both separated and linked together by one molecule of histone H1, also located on the DNA fiber. Active transcription is associated with H1-nucleosomes&horbar;DNA complexes (Banchev et al, 1988). Non-histone nucleoproteins are also involved in the spatial organization of the chromatin (Fredericq, 1976;Bradbury, 1979;Kaye & Wales, 1981;Poccia, 1986;Homberger & Koller, 1988), but their occurrence in young embryos is far from being completely understood.…”

mentioning

confidence: 99%

See 1 more Smart Citation

Immunocytochemical localization of histones H2B, H3 and H4 in pronuclei and four-cell stages of porcine embryos. Preliminary results

Rozinek¹,

Muller²,

Courtens³

1989

Reprod. Nutr. Dévelop.

View full text Add to dashboard Cite

Summary ― In this preliminary work, using pig embryos ultrastructural immunocytochemistry with polyclonal antibodies against purified histones was used to demonstrate both their localization and the time of their appearance in pronuclei, from 15 h after ovulation (pronuclear stage) to 48 h postinsemination (4-cell stage).In pronuclei, the histones H2B, H3, and H4 were located in the heterochromatin as soon as it appeared. Usually, one of the pronuclei seemed to be more heavily labelled. The chromatin facing the zone of pronuclear contact formed a bowl-shaped region in each pronucleus heavily labelled for these histones. The so-called pseudo-nucleoli were present in both pronuclei and contained H2B.In 4-cell stages, the labelling intensities of heterochromatin for H2B, H3 and H4 were equal in all the nuclei. H2B was still evident in the pseudo-nucleoli, but in a lower quantity than before. The condensed chromatin located either under the nuclear envelope or surrounding the pseudo-nucleoli was heavily labelled for H2B, H3 and H4.

show abstract

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

Immunocytochemical localization of histones H2B, H3 and H4 in pronuclei and four-cell stages of porcine embryos. Preliminary results

Rozinek¹,

Muller²,

Courtens³

1989

Reprod. Nutr. Dévelop.

View full text Add to dashboard Cite

show abstract

“…In addition to a number of other pre-existing H1 subtypes, histone H1 0 appears in cells, during terminal differentiation (3, 4) or after growth inhibition (5,6). Although the role of this linker histone remains unclear, it has been proposed to localize specifically to the periphery of nucleus (7). Like other replacement histones, H1 0 accumulates in postmitotic cells and is synthesized in the absence of DNA replication (8 -11); however, transcription of the H1 0 gene seems to be a replication-dependent event, at least in some cell types (12,13).…”

Section: During Brain Maturation Histone H1mentioning

confidence: 99%

H10 RNA-binding Proteins Specifically Expressed in the Rat Brain

Scaturro¹,

Nastasi²,

Raimondi³

et al. 1998

Journal of Biological Chemistry

View full text Add to dashboard Cite

During brain maturation, histone H10 accumulates in both nerve and glial cells. The expression of this "linker" histone, the role of which still remains unclear, is a complex process, having both transcriptional and posttranscriptional regulatory components. In particular, the expression of H1 0 in rat cortical neurons is regulated mainly at the post-transcriptional level, and unknown cellular proteins are likely to affect H1 0 mRNA stability and/or translation. In looking for such factors, we tested the ability of rat brain extracts to protect H1 0 RNA probe from degradation by T1 RNase. The results reported here demonstrate that rat brain contains at least one major (p40) and two minor (p110 and p70) binding factors, specific for H1 0 RNA, all of which are much more or exclusively expressed in adult rat brain, when compared with other tissues. The binding of the factors is confined to a portion of the 3-untranslated region (3-UTR), which is highly conserved among murine and human H1 0 mRNAs. These findings suggest that the proteins identified play a critical role in regulating the expression of H1 0 histone in the brain of mammals.During development and differentiation, cells undergo precise sequences of events that imply switching on or off different sets of genes, and even terminally differentiated cells respond to ever changing environmental conditions by modulating the transcriptional activity of many genes. As this often implies the need for remodeling chromatin (for review, see Ref. 1), it is not surprising that non-allelic isotypes of histones are synthesized in differentiated cells and enter chromatin, probably at topologically defined regions of the nucleus.The H1 class of histones, also known as linker histones, are involved in organizing chromatin higher structures as well as in regulating specific gene expression (for discussion, see Ref.2). In addition to a number of other pre-existing H1 subtypes, histone H1 0 appears in cells, during terminal differentiation (3, 4) or after growth inhibition (5, 6). Although the role of this linker histone remains unclear, it has been proposed to localize specifically to the periphery of nucleus (7). Like other replacement histones, H1 0 accumulates in postmitotic cells and is synthesized in the absence of DNA replication (8 -11); however, transcription of the H1 0 gene seems to be a replication-dependent event, at least in some cell types (12, 13). Regulation of H1 0 expression is thus likely to be a complex process with both transcriptional and post-transcriptional components.In maturing brain, H1 0 accumulation was demonstrated in both neurons (11, 14 -16) and glial cells (9). However, the role of H1 0 in gene expression remains unclear. We previously cloned two cDNAs encoding rat histones H1 0 (17) and H3.3 (14), respectively. We used these cDNAs as probes to study the accumulation of the corresponding messages during rat brain development (14) and in cultured neurons (18). The effects of transcriptional inhibition by actinomycin D and the results of nuclea...

show abstract

“…However, H1" expression is detected at a basal level in several tumor-cell lines, e.g. Friend cells [14], F9 cells [15] or HeLa cells [16]. In HepG2, H1" is constitutively synthesized at a high level [17].…”

mentioning

confidence: 99%

Differential regulation of the human H1°‐histone‐gene transcription in human tumor‐cell lines

Bouterfa

Triebe

Doenecke

1993

European Journal of Biochemistry

View full text Add to dashboard Cite

Cloning and sequence analysis of about 2 kb of the 5' flanking region of the human H1 " histone gene reveals several potential regulatory elements upstream of the transcribed portion of this gene. Transfection studies using the chloramphenicol acetyl tranferase (CAT) gene as a reporter gene with a series of promoter deletions revealed that the expression of the H1" gene may depend on a complex interplay of several transcription factors, including members of the retinoic acid and/or thyroid-hormone-receptor superfamily, at the 5' flanking region of the H1" gene. CAT assays demonstrate varied patterns of expression and regulation in different human tumor-cell lines. The leukemia cell line HL60 does not express H1" mRNA and shows no CAT activity. HeLa cells strongly express the CAT gene under the control of the H1" promoter. Under the same conditions, HepG2 cells also transcribe the CAT gene, although at a lower rate than HeLa cells. Using different promoter-delction clones, the CAT activity differs in HepG2 and HeLa cells in the very distal promoter region. In both cell lines, the CAT activity decreases several fold when the region between nucleotides -450 and -600 upstream of the mRNA start site is deleted. It also decreases when just the proximal portion but not the distal promoter region is deleted. In summary, the regulatory patterns of these three cell lines differ, indicating a cell-type-specific regulation of the human H1 "-histone-gene expression.The H1 histones, which constitute the most variable group of histone proteins [l], bind to the linker DNA between nucleosome cores and are involved in the formation of higher-order chromatin structures [2]. The availability of different H1 subtypcs may provide a means to modulate such higher-order chromatin structures at specific sites 131. In mammals, at least five different subtypes (Hla-e) constitute the main H1 group [4] ; in addition, spermatogenic cells feature the testis-specific isoform Hlt [5]. The subtype H1" [6], a structural homologue of the avian and amphibian H5 histones, is confined to highly differentiated tissues, such as liver [7]

show abstract

Immunofluorescent localization of histone H10 in the nuclei of proliferating and differentiating friend cells

Cited by 31 publications

References 20 publications

Immunocytochemical localization of histones H2B, H3 and H4 in pronuclei and four-cell stages of porcine embryos. Preliminary results

Immunocytochemical localization of histones H2B, H3 and H4 in pronuclei and four-cell stages of porcine embryos. Preliminary results

H10 RNA-binding Proteins Specifically Expressed in the Rat Brain

Differential regulation of the human H1°‐histone‐gene transcription in human tumor‐cell lines

Contact Info

Product

Resources

About