Sequential phsophorylation of histone subfractions in the Chinese hamster cell cycle.

Gurley, L.R.; Walters, R.A.; Tobey, Robert A.

doi:10.1016/s0021-9258(19)41488-9

Cited by 211 publications

(72 citation statements)

References 34 publications

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“…In mammalian cells, there are zero to one phosphate per histone H1 during the G1 phase of the cell cy-cle, and this increases by another two phosphates during S phase. The level of phosphorylation then rises through G2 up to the hyperphosphorylated state of four to six phosphates per histone H1 at metaphase (17)(18)(19)21). This correlation between histone phosphorylation and chromosome condensation was also observed during the induction of premature chromosome condensation in sea urchin eggs and in mammalian cells (1,27).…”

mentioning

confidence: 74%

The topoisomerase II inhibitor VM-26 induces marked changes in histone H1 kinase activity, histones H1 and H3 phosphorylation, and chromosome condensation in G2 phase and mitotic BHK cells.

Roberge

Th'ng

Hamaguchi

et al. 1990

The Journal of Cell Biology

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Abstract. We have examined the effects of topoisomerase inhibitors on the phosphorylation of histones in chromatin during the G2 and the M phases of the cell cycle. Throughout the G2 phase of BHK cells, addition of the topoisomerase II inhibitor VM-26 prevented histone HI phosphorylation, accompanied by the inhibition of intraceUular histone H1 kinase activity. However, VM-26 had no inhibitory effect on the activity of the kinase in vitro, suggesting an indirect influence on histone H1 kinase activity. Entry into mitosis was also prevented, as monitored by the absence of nuclear lamina depolymerization, chromosome condensation, and histone H3 phosphorylation. In contrast, the topoisomerase I inhibitor, camptothecin, inhibited histone H1 phosphorylation and entry into mitosis only when applied at early G2.In cells that were arrested in mitosis, VM-26 induced dephosphorylation of histones H1 and H3, DNA breaks, and partial chromosome decondensation. These changes in chromatin parameters probably reverse the process of chromosome condensation, unfolding condensed regions to permit the repair of strand breaks in the DNA that were induced by VM-26. The involvement of growth-associated histone HI kinase in these processes raises the possibility that the cell detects breaks in the DNA through their effects on the state of DNA supercoiling in constrained domains or loops. It would appear that histone H1 kinase and topoisomerase II work coordinately in both chromosome condensation and decondensation, and that this process participates in the VM-26-induced G2 arrest of the cell.

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confidence: 74%

The topoisomerase II inhibitor VM-26 induces marked changes in histone H1 kinase activity, histones H1 and H3 phosphorylation, and chromosome condensation in G2 phase and mitotic BHK cells.

Roberge

Th'ng

Hamaguchi

et al. 1990

The Journal of Cell Biology

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“…Both the level and specific sites of phosphorylation have been observed to change in response to development (Billings et al, 1979;Blumenfeld et al, 1978;Green and Poccia, 1985;Lennox et al, 1982;Newrock et al, 1978;Talmadge and Blumenfeld, 1987) or the progression of the cell cycle (Ajiro et al, 1981a(Ajiro et al, ,b, 1983Balhorn et al, 1972;Bradbury et al, 1974a,b;Gurley et al, 1975Gurley et al, , 1978aHohmann et al, 1975Hohmann et al, , 1976Langan, 1982;Y nox and Cohen, 1983). Indeed, a hyperphosphorylation ot rll during mitosis in higher eukaryotes has led to the correlation of such phosphorylation with the condensation of mitotic chromosomes (Balhorn et al, 1972;Bradbury et al, 1974a,b;Gurley et al, 1975Gurley et al, , 1978aInglis et al, 1976;Krystal and Poccia, 1981;Lake et al, 1972;Matsumoto et al, 1980;Paulson and Taylor, 1982;Tanphaichitr et al, 1976). However, HI is phosphorylated at other times during the cell cycle (Ajiro et al, 1981a(Ajiro et al, ,b, 1983Gurley et al, 1975Gurley et al, , 1978aHohmann et al, 1975;Lennox et al, 1982) and in nuclei which do not divide mitotically (Allis and Gorovsky, 1981;Talmadge and Blumenfeld, 1987).…”

mentioning

confidence: 99%

“…Indeed, a hyperphosphorylation ot rll during mitosis in higher eukaryotes has led to the correlation of such phosphorylation with the condensation of mitotic chromosomes (Balhorn et al, 1972;Bradbury et al, 1974a,b;Gurley et al, 1975Gurley et al, , 1978aInglis et al, 1976;Krystal and Poccia, 1981;Lake et al, 1972;Matsumoto et al, 1980;Paulson and Taylor, 1982;Tanphaichitr et al, 1976). However, HI is phosphorylated at other times during the cell cycle (Ajiro et al, 1981a(Ajiro et al, ,b, 1983Gurley et al, 1975Gurley et al, , 1978aHohmann et al, 1975;Lennox et al, 1982) and in nuclei which do not divide mitotically (Allis and Gorovsky, 1981;Talmadge and Blumenfeld, 1987). Therefore, phosphorylation of H1 must serve other functions as well, possibly in the regulation of transcription or replication.…”

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confidence: 99%

Characterization of phosphorylation sites in histone H1 in the amitotic macronucleus of Tetrahymena during different physiological states.

Roth

Schulman

Richman

et al. 1988

The Journal of Cell Biology

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Abstract. Histone H1 is highly phosphorylated in transcriptionally active, amitotic macronuclei of Tetrahymena during vegetative growth. However, the level of H1 phosphorylation changes dramatically in response to different physiological conditions. H1 is hyperphosphorylated in response to heat shock and during prezygotic stages of conjugation. Conversely, H1 is largely dephosphorylated during prolonged starvation and during elimination of parental macronuclei during conjugation. Mapping of phosphorylation sites within HI indicates that phosphorylation occurs at multiple sites in the amino-terminal portion of the molecule, predominantly at threonine residues. Two of these sites have been identified by compositional analyses and microsequencing of tryptic peptides. Interestingly, two major sites contain the sequence Thr-ProVal-Lys similar to that contained in the sites recognized by growth-associated histone kinase in other organisms. No new sites are detected during the hyperphosphorylation of H1 which occurs during heat shock or in early stages of conjugation, and no sites are preferentially dephosphorylated during starvation or later stages of conjugation. Therefore, changes in the overall level of H1 phosphorylation, as opposed to phosphorylation or dephosphorylation at particular sites, appear to be important in the regulation of chromatin structure under these physiological conditions. Further, since no cell division or DNA replication occurs under these conditions, changes in the level of H1 phosphorylation are best correlated to changes in gene expression during heat shock, starvation, and conjugation. We suggest that, at least in Tetrahymena, H1 hyperphosphorylation is used as a rapid and transient mechanism for the cessation of transcription under conditions of cellular stress.

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“…CHO cells were seeded in 100-mm dishes for luciferase assays, immunoblotting, and immunoprecipitation; 150-mm tissue culture dishes were used for fluorescence-activated cell sorter analysis; and 6-well multidish plates were used for the analysis of [3H]thymidine incorporation. Log-phase cultures were synchronized at the G1/S boundary by treatment for 18 h with 1 ,ug of aphidicolin per ml or 1 mM hydroxyurea, washed three times with serum-free medium, transferred to complete medium for 10 h, and then growth arrested by incubation in medium containing aphidicolin or hydroxyurea for 18 h. Hydroxyurea arrests cells near the GJ/S boundary at a point distinct from aphidicolin arrest (1,26,46,81,118). To arrest cells in the G2 phase, the cells were presynchronized at G1/S by treatment with 1 mM hydroxyurea for 18 h, washed three times with serum-free medium, and then incubated for an additional 12 h in complete medium supplemented with 7.5 p,g of Hoechst 33342 dye per ml (113).…”

Section: Methodsmentioning

confidence: 99%

Cell Cycle Regulation of the c-Myc Transcriptional Activation Domain

Seth

Gupta

Davis

1993

Molecular and Cellular Biology

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The product of the c-myc gene (c-Myc) is a sequence-specific DNA-binding protein that has previously been demonstrated to be required for cell cycle progression. Here we report that the c-Myc DNA binding site confers cell cycle regulation to a reporter gene in Chinese hamster ovary cells. The observed transactivation was biphasic with a small increase in G1 and a marked increase during the S-to-G2/M transition of the cell cycle. This cell cycle regulation of transactivation potential is accounted for, in part, by regulatory phosphorylation of the c-Myc transactivation domain. Together, these data demonstrate that c-Myc may have an important role in the progression of cells through both the G1 and G2 phases of the cell cycle.

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Sequential phsophorylation of histone subfractions in the Chinese hamster cell cycle.

Cited by 211 publications

References 34 publications

The topoisomerase II inhibitor VM-26 induces marked changes in histone H1 kinase activity, histones H1 and H3 phosphorylation, and chromosome condensation in G2 phase and mitotic BHK cells.

The topoisomerase II inhibitor VM-26 induces marked changes in histone H1 kinase activity, histones H1 and H3 phosphorylation, and chromosome condensation in G2 phase and mitotic BHK cells.

Characterization of phosphorylation sites in histone H1 in the amitotic macronucleus of Tetrahymena during different physiological states.

Cell Cycle Regulation of the c-Myc Transcriptional Activation Domain

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