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

Bouterfa, Hakim; Triebe, Suzane; Doenecke, Detlef

doi:10.1111/j.1432-1033.1993.tb18253.x

Cited by 24 publications

(26 citation statements)

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“…Duncliffe et al [27] showed, by reportergene analysis, that this element was needed for enhanced expression of a chicken H1 gene promoter. This finding explained, in retrospect, the data that had been obtained in promoter studies with H1°histone gene promoters from mouse [46], Xenopus laevis [28] and man [51]. These reports described an upstream conserved sequence (UCE I [28]) that contained the CH1UE motif.…”

Section: Discussionmentioning

confidence: 75%

Conserved sequence elements in human main type‐H1 histone gene promoters : their role in H1 gene expression

Meergans¹,

Albig²,

Doenecke³

1998

European Journal of Biochemistry

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In man, the H1 class of histones consists of seven different isoforms, termed H1.1ϪH1.5, H1t and H1°. Analysis of the promoters of the respective genes reveals that all seven H1 gene promoters share conserved sequence elements: a TATA box at around position Ϫ25 (relative to the transcription start site), a CCAAT motif at about position Ϫ50 (except in the H1 promoter), an H1-box (AAACACA) around position Ϫ110 (except in the H1.1 promoter), and the highly conserved motif TGTGT/CTA (TG-box or CH1UE) at around nucleotide position Ϫ450 (except in the H1.1 promoter). Analysis of the H1.3 gene promoter was carried out with reporter gene assays (using the luciferase gene as a reporter gene) including stepwise deletion and site-directed mutagenesis. In addition, electrophoretic mobility-shift assays were carried out for the analysis of protein/DNA interactions at conserved promoter motifs. Mutation analysis indicates that the CH1UE motif is involved in mediating the S-phase-dependent expression of the H1.3 gene. Comparison of H1 promoters shows that the CCAAT-box is extended in each case by CA. Mutational analysis indicates that only the CCAATCA heptanucleotide, but not just the CCAAT sequence mediates the effect of this element in H1 gene promoters.Keywords : histone H1; histone gene promoter; (histone) gene expression ; gene regulation; luciferase activity.Histones are a major component in the eukaryotic nucleus and play an important role in forming the fundamental nucleosomal subunit structure of chromatin. They are subdivided into the group of core histones (H2A, H2B, H3 and H4), which form the histone octamer of the nucleosomal core and the group of H1-linker histones. These H1 histones seal two rounds of DNA at the surface of the core-histone octamer [1], influence the positioning of nucleosomes [2,3] and are essential for the formation of higher order chromatin structures [4]. In addition, H1 histones exert general inhibitory effects on transcription [5,6], but can also play a specific role in gene regulation [7Ϫ9].In mammals, the group of H1 histones consists of at least seven different subtypes. The H1 histones represent the most variable class of the otherwise highly conserved histone proteins. Based on both the timing of synthesis relative to the cell cycle and their tissue-specific occurrence, the H1 histones can be classified into three different groups of subtypes : (a) the main type-H1 histones, which are expressed in close relation to the S phase of the cell cycle ; (b) the replacement subtype H1, which is usually expressed in highly differentiated cells and (c) the subtype H1t which is expressed exclusively in the testis [10].

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Section: Discussionmentioning

confidence: 75%

Conserved sequence elements in human main type‐H1 histone gene promoters : their role in H1 gene expression

Meergans¹,

Albig²,

Doenecke³

1998

European Journal of Biochemistry

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“…Experiments performed on MEL, B16 and HTC cells showed that H18 mRNA accumulation resulted from an increase of H18 transcription rate [3,4,7], which did not require protein synthesis when stimulated by either HMBA [7] or sodium butyrate [4]. Although the H18 promoter has been isolated from mouse [8], Xenopus laevis [9], human [10] and rat [11], little is known about factors involved in the regulation of the gene. We have recently shown that sodium butyrate activates H18 gene expression in HTC cells by modulating a serine/threonine phosphatase activity [4].…”

mentioning

confidence: 99%

Quantitative analysis of histone H1° protein synthesis in HTC cells

Cuisset

Tichonicky

Delpech

1999

European Journal of Biochemistry

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H18, a member of histone H1 family associated with cell growth arrest and differentiation, is barely expressed in most mammalian cells in culture. Depending on the cell type, serum deprivation or drugs, such as sodium butyrate, significantly increase H18 mRNA level and H18 protein accumulates. However, probably because of a lack of a simple quantitative procedure, little is known about the relationship between H18 mRNA content and its effective translation rate. Using a rat hepatoma cell line and sodium butyrate as a model system, we attempted to evaluate this in different cellular conditions by measuring H18 synthesis with a rapid quantitative procedure we described previously. We found that although the amount of H18 mRNA rapidly increased and then stabilized under sodium butyrate treatment, its transcription was delayed and H18 protein was synthesized in a progressive wave. Butyrate removal from cell culture confirmed that mRNA level and protein synthesis were independently regulated, and provided evidence that sodium butyrate would not directly target the translation apparatus. In contrast, during the S phase of the cell cycle, H18 gene transcription and protein synthesis were concomitantly activated. Taken together these data provide evidence that H18 accumulation results from an increase of its synthesis and that, depending on conditions, a cell exhibits a H18 translation efficiency which may or may not reflect the mRNA level.Keywords: histone H18; sodium butyrate; ion-exchange HPLC. Histone H18 was first described in 1969 by Panyim and Chalkley as an H1-like protein, typically found in tissues with little or no cell proliferation [1]. Cell growth arrest or differentiation induced by either serum deprivation or drugs, including sodium butyrate, hexamethylene bis-acetamide (HMBA) and dimethyl sulfoxide, were shown to increase H18 mRNA and protein levels in most mammalian cells in culture. Sodium butyrate induction led to the rapid accumulation of a 2.2-kb H18 mRNA in HeLa cells [2], B16 murine melanoma cells [3] and rat hepatoma tissue culture (HTC) cells used in this study [4]. Unlike HeLa and B16 cells which are stimulated to differentiate, HTC cells are progressively blocked at the early G1 phase of the cell cycle under sodium butyrate treatment [5,6]. Because this effect is reversible upon removal of the inducer, a 24-h sodium butyrate treatment can therefore be used for HTC cell synchronization [5]. Experiments performed on MEL, B16 and HTC cells showed that H18 mRNA accumulation resulted from an increase of H18 transcription rate [3,4,7], which did not require protein synthesis when stimulated by either HMBA [7] [4]. In the MEL cell line, H18 mRNA preferentially accumulates in mid or late S phase, even when cells have been pulse-induced by a 2-h treatment with HMBA [12,13]. Such a specific accumulation has also been observed during rat liver regeneration [14].Numerous studies have shown that drug-treatment induced H18 protein accumulation in mammalian cells in culture. Treatment of MEL cells with HMBA...

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“…In addition to the TATA box, the H1 box, and an Spl site (see above), the H1" promoter of mouse and man contains a binding site for the retinoic acid receptor [Breuer et al, 1989[Breuer et al, , 1993Bouterfa et al, in press] and other conserved sequence motifs within otherwise divergent promoter sequences. The presence of a retinoic acid receptor binding site agrees with the induction of differentiation of murine F9 cells, which is induced by retinoic acid and includes the synthesis of H1" mRNA and protein [Alonso et al, 19881.…”

Section: H14mentioning

confidence: 99%

Organization and expression of H1 histone and H1 replacement histone genes

Doenecke

Albig

Bouterfa

et al. 1994

J of Cellular Biochemistry

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The H I family is the most divergent subgroup of the highly conserved class of histone proteins [Cole: Int J Pept Protein Res 30:433-449, 19871. In several vertebrate species, the H I complement comprises five or more subtypes, and tissue specific patterns of H I histones have been described. The diversity of the H I histone family raises questions about the functions of different H I subtypes and about the differential control of expression of their genes. The expression of main type H I genes is coordinated with DNA replication, whereas the regulation of synthesis of replacement H I subtypes, such as H I " and H5, and the testis specific H I t appears to be more complex. The differential control of H I gene expression is reflected in the chromosomal organization of the genes and in different promoter structures. This review concentrates on a comparison of the chromosomal organization of main type and replacement H I histone genes and on the differential regulation of their expression. General structural and functional data, which apply to both H I and core histone genes and which are covered by recent reviews, will not be discussed in detail.1994 WtIey-Liss, Inc

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

Cited by 24 publications

References 59 publications

Conserved sequence elements in human main type‐H1 histone gene promoters : their role in H1 gene expression

Conserved sequence elements in human main type‐H1 histone gene promoters : their role in H1 gene expression

Quantitative analysis of histone H1° protein synthesis in HTC cells

Organization and expression of H1 histone and H1 replacement histone genes

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