Syntheses and modulations in the chromatin contents of histones H1.degree. and H1 during G1 and S phases in Chinese hamster cells

D'Anna, Joseph A.; Gurley, L.R.; Tobey, Robert A.

doi:10.1021/bi00260a014

Cited by 46 publications

(47 citation statements)

References 51 publications

(48 reference statements)

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“…As an internal control (Fig. SE), the same RNA preparations were assayed for the levels of a cell cycle-dependent H4 histone mRNA by using a S'-end-labeled probe derived from XHHG41 (11 4. Structure of pSVP2AHEN consists of the 5'-flanking region, the first 20 nucleotides ofthe leader sequence from the human H3 histone gene (from pST519) (9,16,17), the first and second exons, the first intron of the human ,B-globin gene, and the simian virus 40 early polyadenylylation sequence.…”

Section: Construction and Expression Of A Heatmentioning

confidence: 99%

“…It has been well established that histone gene expression and DNA replication are temporally and functionally coupled. The synthesis of most histone proteins (1)(2)(3)(4)(5)(6) and the steadystate levels of histone mRNAs (7)(8)(9)(10)(11)(12) are closely correlated with DNA synthesis in the S phase of the cell cycle. At the natural end of S phase or following inhibitor-induced termination of DNA synthesis, there is a coordinate and stoichiometric decrease in histone mRNA levels and histone protein synthesis (8)(9)(10)(11)(12)(13).…”

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confidence: 99%

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Involvement of the 5'-leader sequence in coupling the stability of a human H3 histone mRNA with DNA replication.

Morris¹,

Marashi²,

Weber³

et al. 1986

Proc. Natl. Acad. Sci. U.S.A.

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Two lines of evidence derived from fusion gene constructs indicate that sequences residing in the 5'-nontranslated region of a cell cycle-dependent human H3 histone mRNA are involved in the selective destabilization that occurs when DNA synthesis is terminated. The experimental approach was to construct chimeric genes in which fragments of the mRNA coding regions of the H3 histone gene were fused with fragments of genes not expressed in a cell cycle-dependent manner. After transfection in HeLa S3 cells with the recombinant plasmids, levels of fusion mRNAs were determined by S1 nuclease analysis prior to and following DNA synthesis inhibition. When the first 20 nucleotides of an H3 histone mRNA leader were replaced with 89 nucleotides of the leader from a Drosophila heat-shock (hsp70) mRNA, the fusion transcript remained stable during inhibition of DNA synthesis, in contrast to the rapid destabilization of the endogenous histone mRNA in these cells. In a reciprocal experiment, a histone-globin fusion gene was constructed that produced a transcript with the initial 20 nucleotides of the H3 histone mRNA substituted for the human f3-globin mRNA leader. In HeLa cells treated with inhibitors of DNA synthesis and/or protein synthesis, cellular levels of this histone-globin fusion mRNA appeared to be regulated in a manner similar to endogenous histone mRNA levels. These results suggest that the first 20 nucleotides of the leader are sufficient to couple histone mRNA stability with DNA replication.The human histone genes are a moderately repeated gene family that encode the major structural proteins ofchromatin. It has been well established that histone gene expression and DNA replication are temporally and functionally coupled. The synthesis of most histone proteins (1-6) and the steadystate levels of histone mRNAs (7-12) are closely correlated with DNA synthesis in the S phase of the cell cycle. At the natural end of S phase or following inhibitor-induced termination of DNA synthesis, there is a coordinate and stoichiometric decrease in histone mRNA levels and histone protein synthesis (8)(9)(10)(11)(12)(13). The rapid loss of histone mRNA under these conditions is in contrast to minimal changes in nonhistone mRNA levels. The selective destabilization of histone mRNA during DNA synthesis inhibition is posttranscriptionally mediated; destabilization is not dependent on transcription (11) but requires protein synthesis (11-15). The cellular and molecular basis for histone mRNA turnover, however, remains unresolved.To address molecular mechanisms operative in the selective destabilization of histone mRNAs, we are attempting to identify regions of a cloned, cell cycle-dependent human H3 histone gene (16,17) that are involved in the destabilization of its transcripts. Our approach is to construct fusion genes, in which fragments ofthe mRNA coding regions ofthe cloned human H3 histone gene are fused with fragments of other genes not expressed in a cell cycle-dependent manner. After transfection into HeLa S3 cells, le...

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Section: Construction and Expression Of A Heatmentioning

confidence: 99%

mentioning

confidence: 99%

Involvement of the 5'-leader sequence in coupling the stability of a human H3 histone mRNA with DNA replication.

Morris¹,

Marashi²,

Weber³

et al. 1986

Proc. Natl. Acad. Sci. U.S.A.

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“…In most eukaryotic cells, there is a temporal relationship between histone protein synthesis, histone mRNA synthesis, and DNA replication (22)(23)(24)(25)(26)(27)(28)(29)(30). The accumulation of histone mRNA parallels DNA synthesis, while histone transcription rates peak in early S phase (30)(31)(32).…”

mentioning

confidence: 99%

A human histone H4 gene exhibits cell cycle-dependent changes in chromatin structure that correlate with its expression.

Chrysogelos¹,

Riley²,

Stein³

et al. 1985

Proc. Natl. Acad. Sci. U.S.A.

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By use of synchronized human HeLa S3 cells, a site sensitive to both DNase I and nuclease S1 was identified 50-150 base pairs upstream of the ATG codon of a cell cycle-dependent histone H4 gene. This site expanded to include a broad region of -30O base pairs sensitive to DNase I throughout S phase and then narrowed again to the original site after the completion of DNA replication. The level of nuclease S1 sensitivity was greatest during early S phase, when the gene is replicated and its transcription rate is maximal. The chromatin structure of the human fglobin gene, which is not expressed in HeLa cells, was also analyzed throughout the cell cycle, and in no case was a sub-band seen as a result of DNase I or nuclease S1 digestion, nor were there any changes in nuclease sensitivity correlated with its replication. Thus the cell cycle-dependent chromatin alterations in this histone H4 gene appear to be due to the coupled replication and expression of this gene rather than simply its replication. These results suggest that histone genes, as compared with developmentally regulated genes, exhibit an "intermediate" level of regulation whereby the gene is never in a completely inactive conformation, but changes in chromatin structure occur as a function of the cell cycle and expression.Changes in the structural organization of chromatin play an important role in determining the transcriptional state of eukaryotic genes (1-6). Active chromatin characteristically exhibits increased susceptibility to nucleases (7-9), and short regions hypersensitive to DNase I and/or nuclease S1 commonly occur near the 5' end of active or potentially active genes (1, 10-13), suggesting a role for these sites in the regulation of gene expression. The correlation between changes in chromatin structure and the activation or inactivation of eukaryotic genes has been reported for developmentally controlled genes (9, 14-16) or genes under hormonal control (17-21). Here we present evidence that a cell cycleregulated human histone H4 gene undergoes chromatin alterations during the cell cycle that reflect its expression.The histone genes offer an excellent opportunity to examine the potential chromatin reconfigurations of cell cycledependent genes. In most eukaryotic cells, there is a temporal relationship between histone protein synthesis, histone mRNA synthesis, and DNA replication (22-30). The accumulation of histone mRNA parallels DNA synthesis, while histone transcription rates peak in early S phase (30-32). Additionally, following the inhibition of DNA synthesis and, consequently, of histone gene expression, recovery involves the "remembering" of the specific position of the cell in S phase (29,33,34).The histone H4 gene used in these studies (designated pFO108A) has been well characterized and has been shown to be expressed in a cell cycle-dependent manner (30,33,35). We have identified a site sensitive to both DNase I and nuclease S1 in the 5' flanking region of this gene, using HeLa S3 cells synchronized by a double thymidine blo...

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“…5 B). Lymphocytes do not contain or synthesize Hl" in [24] and D'Anna et al [40,41], who respectively reported differential synthesis of H1 variants in synchronized S-phase HeLa cells and synchronized Chinese hamster ovary cells.…”

Section: H I ' Synthtsismentioning

confidence: 99%

H1 variant synthesis in proliferating and quiescent human cells

D’Incalci

Allavena

et al. 1986

Eur J Biochem

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The synthesis of histone HI isoprotein species in human cells of several different types and in several different physiological states was studied. U p to five H1 and two H1" isoprotein species could be resolved by twodimensional electrophoresis. All five HI isoprotein species were synthesized in exponentially growing cultures of IMR-90 human fibroblasts; in quiescent IMR-90 cells the synthesis of three HI isoprotein species was greatly decreased while the synthesis of two others was much less affected. When DNA synthesis in exponentially growing cultures of IMR-90 was inhibited, the pattern of HI isoprotein synthesis became similar to that found in quiescent cultures. Other human cells, isolated from blood, yielded similar results. These results suggest that the pattern of HI synthesis is the same for cells in non-S phases of the cell cycle and in quiescent cells. Thus for histone H1 in human cells the relationship of the variant synthesis pattern to the growth state and DNA replication is similar to that of the core histone H3 but not that of H2A.Recent studies have demonstrated that core histone synthesis does not occur exclusively in the S phase of the cell cycle; a decreased but significant amount also occurs in other phases of the cell cycle as well as in quiescent cells (GO) [I, 21. The variant pattern of core histone (includes H3, H4, H2A, and H2B, but not H1) synthesis is different in each of these various physiological states (S, GI, or GO phase). All variants are synthesized in S phase. The H3 variants H3.1 and H3.2 are not synthesized during either G1 or GO. The H2A variants H2A.1 and H2A.2 are synthesized in GO (as in S), but not in cells synchronized in G1 or treated with drugs which inhibit DNA synthesis [l -31. Thus, cells in G1 or GO show a similar pattern of H3 histones but differ from each other in the pattern of H2A synthesis.Histone H1 is also known to be composed of a family of isoprotein species possessing microheterogeneity in their sequences (see reviews [4, 51). The majority of early studies report the presence of two H1 variants (H1A + H1B) in addition to HI" [6 -131. Recently Lennox et al. [14] used twodimensional gel electrophoresis to identify five HI species present in murine teratocarcinoma cell lines and in normal tissues derived from mice, rats, pigs and cows.The exact relationship between DNA synthesis and H1 variant synthesis, however, remains unclear because many early studies [I 5 -231 were performed using one-dimensional sodium dodecyl sulfate (SDS) gel electrophoresis or gel filtration chromatography, neither of which possesses a sufficient degree of resolving power to properly separate H1 subtypes with similar molecular masses. Nevertheless the data do suggest that the regulation of synthesis of H1 variants may resemble that of the core histone variants. Gurley and Hardin [I81 and Apels and Ringertz [19, 201 reported have shown that the variants of H1 are synthesized at unequal rates 231 and turnover at unequal rates [13, 211. Sizemore and Cole [24] reported th...

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Syntheses and modulations in the chromatin contents of histones H1.degree. and H1 during G1 and S phases in Chinese hamster cells

Cited by 46 publications

References 51 publications

Involvement of the 5'-leader sequence in coupling the stability of a human H3 histone mRNA with DNA replication.

Involvement of the 5'-leader sequence in coupling the stability of a human H3 histone mRNA with DNA replication.

A human histone H4 gene exhibits cell cycle-dependent changes in chromatin structure that correlate with its expression.

H1 variant synthesis in proliferating and quiescent human cells

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