Occurrence and properties of a chromatin-associated Fl-histone phosphokinase in mitotic Chinese hamster cells

Lake, Robert S.; Salzman, Norman P.

doi:10.1021/bi00775a027

Cited by 141 publications

(45 citation statements)

References 29 publications

(16 reference statements)

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“…The observation that chromatin isolated from micronuclei does not contain any detectable histone fraction F1 reinforces our previous suggestion (10) that histone F1 and its phosphorylation do not function uniquely in the process of mitotic chromosome condensation (16,(21)(22)(23). Thus, histone fraction F1 is present and is phosphorylated in macronuclei, which divide amitotically, with little or no change in chromatin organization; F1 is absent in micronuclei, which divide mitotically and show distinct changes in chromatin condensation during the cell cycle (2-7).…”

Section: Discussionsupporting

confidence: 90%

“…Thus, the relationship between the rate of cell replication and the extent of phosphorylation of histone F1 observed in a variety of other cell types (11)(12)(13)(14)(15)(16) was also observed in Tetrahymena. Recent studies of histone phosphorylation in different cells have led to the various suggestions that phosphorylation of histone F1 may be involved in the alteration of chromatin structure during interphase (17), in chromosome replication (18,19), in the sorting out of newly synthesized chromatids during S-phase (20), in the process of mitotic chromosome condensation (21)(22)(23) or in the control of genetic activity (24)(25)(26). Since MATERIALS AND METHODS Cell Culture.…”

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confidence: 99%

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Absence of histone F1 in a mitotically dividing, genetically inactive nucleus.

Gorovsky¹,

Keevert²

1975

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

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Histones were extracted from macro-and micronuclear chromatin of the ciliated protozoan Tetrahymena pyriformis. Conditions that resulted in macronuclear chromatin containing large amounts of histone F1 yielded micronuclear chromatin in which this histone was absent. Evidence is presented indicating that the absence of F1 from micronuclei is not a preparative artifact and that histone F1 is replaced by other tistone fractions. Since micronuclei divide mitotically, while macronuclei divide amitotically, these results suggest that histone F1 and its phosphorylation do not play an indispensable role in the process of mitotic chromosome condensation, in chromosome replication, or in the separation of newly synthesized chromatids. Like most ciliated protozoans, the vegetative cells of Tetrahymena pyriformis contain a macro-and a micronucleus. These two nuclei are formed from the daughter products of a single mitotic division during the sexual process of conjugation. It is likely, therefore, that they contain the same, or closely related, genetic information. In spite of their common origin and the fact that they reside in the same cytoplasmic millieu, macro-and micronuclei differ considerably in their structure and function (see ref. 1 for review). For example, macronuclei divide amitotically, with no sign of mitotic chromosomes; micronuclei divide mitotically (2-7). In addition, the two nuclei differ greatly in their genetic activity. Macronuclei are sites of intense RNA synthesis while micronuclei synthesize little, if any, detectable RNA (8, 9).We have recently reported that the macronucleus of Tetrahymena contains a histone with properties similar to those of histone F1 of higher organisms (10). Macronuclear F1 isolated from rapidly growing cells was found to be highly phosphorylated, while histones isolated from slowly growing cells contained only small amounts of phosphorylated FL. Thus, the relationship between the rate of cell replication and the extent of phosphorylation of histone F1 observed in a variety of other cell types (11)(12)(13)(14)(15)(16) MATERIALS AND METHODS Cell Culture. Tetrahymena pyriformis, strains WH-6 (Syngen 1, mating type I; a micronucleate strain) and GL (an amicronucleate strain), were cultured as described (27).Isolation of Nuclei and Chromatin. Nuclei were isolated as described (27,28). Chromatin was isolated by a modification of the method of Panyim et al. (29). Chromatin deficient in histone fraction F1 was prepared by washing isolated nuclei repeatedly in 0.5 M NaCl. This treatment was found to remove most of histone F1 from macronuclei while extracting little of the other histone fractions.Isolation of Histones. Histones were isolated from whole nuclei or from chromatin by extraction with either 2.4 M urea/0.2 M H2SO4 or with 0.2 M H2SO4 (10, 27).Thermal Denaturation of Isolated Chromatin. Solubilized macro-or micronuclear chromatin was fixed in 0.91% formaldehyde for at least 15 hr and then dialyzed for at least 5 hr against three changes (100 volumes each) of 0.2 mM ...

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Section: Discussionsupporting

confidence: 90%

mentioning

confidence: 99%

Absence of histone F1 in a mitotically dividing, genetically inactive nucleus.

Gorovsky¹,

Keevert²

1975

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

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“…1-3, 5, 6). To determine whether these functions contributed, at least in part, to the smaller size of the Ras/ATF3 ϩ/ϩ tumors than the Ras/ATF3 Ϫ/Ϫ tumors, we assayed the tumors by immunohistochemistry for proliferation using antibody against phosphohistone H3, a mitotic marker (33,34), and for apoptosis using antibody against activated caspase 3, an apoptotic marker. As shown in Fig …”

Section: Ras/atf3mentioning

confidence: 99%

Activating Transcription Factor 3, a Stress-inducible Gene, Suppresses Ras-stimulated Tumorigenesis

Lü

Wolfgang²,

Hai

2006

Journal of Biological Chemistry

175

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ATF3 is a stress-inducible gene that encodes a member of the ATF/CREB family of transcription factors. Current literature indicates that ATF3 affects cell death and cell cycle progression. However, controversies exist, because it has been demonstrated to be a negative or positive regulator of these processes. We sought to study the roles of ATF3 in both cell death and cell cycle regulation in the same cell type using mouse fibroblasts. We show that ATF3 promotes apoptosis and cell cycle arrest.

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“…However, we still do not have much downstream information after enzyme activation, for example, regarding how this is involved in chromatin condensation. For a complete understanding of chromosome condensation, it is necessary to examine critically the phosphorylation of possible substrates related to chromosome condensation together with p34'd'2/H1 kinase activity.Histone HI is a major chromosomal structural protein known to be phosphorylated in a cell-cycle-dependent manner at serine or threonine residues in the SeriThr-Pro-Xaa-Lys and analogous amino acid sequences [11] level of H3 phosphorylation occurring at the 10th serine residue [16, 171 is evident only in M phase [18, 191 or during premature chromosome condensation [20, 211. We earlier indicated that H3 phosphorylation is specific to premature chromosome condensation since (a) H3 is dephosphorylated when the condensation is reversed without dephosphorylation of H1 [22], and (b) H3 is phosphorylated but H1 is dephosphorylated in the later stages of premature chromosome condensation induced by okadaic acid [23].…”

mentioning

confidence: 99%

Vanadate Triggers the Transition from Chromosome Condensation to Decondensation in a Mitotic Mutant (tsTM13)

Ajiro

Yasuda

Tsuji³

1996

European Journal of Biochemistry

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At the nonpermissive temperature (39 "C), chromosomes remain condensed in a temperature-sensitive cell mutant (tsTM13) arrested in the late stage of mitosis. Highly increased activity of histone H1 kinase, hyperphosphorylation of histone H1, and mitosis-specific histone H3 phosphorylation are maintained, even in telophase. In the present study, the defect of chromosome decondensation in tsTM13 cells was found to be partially normalized by a tyrosine phosphatase inhibitor, vanadate, with induction of chromosome decondensation and the formation of multinucleated cells. In the presence of vanadate, the H1 kinase activity dropped to near normal levels and the amount of the inactive form of p3QdcZ protein phosphorylated at a tyrosine residue was increased. H1 and H3 were also extensively de-phosphorylated, the latter being tightly associated with chromosome decondensation. Serinehhreonine-protein phosphatase in late mitosis of the mutant works normally at 39°C. The results indicate that (a) the genetic defect in the mutant may be involved in the control mechanism of the ~34"~'*/Hl kinase activity in the late M phase rather than the phosphatase, (b) normalization of the defect of the mutant by vanadate results from inactivation of H1 kinase, and (c) late mitosis-specific events (p34"d"Z/H1 kinase inactivation, mitosisspecific dephosphorylation of histone H1 and H3) are closely operating with chromosome decondensation.Keywords: vanadate; chromosome decondensation ; cdc2/H1 kinase; histone H3 ; mitosis.The dynamics of the initiation of chromatin condensation at the transition from G2 to M phases and the M to G I phase decondensation during the eukaryotic cell cycle are not fully understood. Analysis of the reversibility of chromosome condensation is crucial for the study of cell cycle regulation and proliferation. It is highly probable that these reversible processes are controlled by a protein phosphorylation-dependent mechanism due to the balance of protein kinase and protein phosphatase activities [I 3. p34"d"2/H1 kinase activation correlates with the initiation and maintenance of M phase [2-41. However, we still do not have much downstream information after enzyme activation, for example, regarding how this is involved in chromatin condensation. For a complete understanding of chromosome condensation, it is necessary to examine critically the phosphorylation of possible substrates related to chromosome condensation together with p34'd'2/H1 kinase activity.Histone HI is a major chromosomal structural protein known to be phosphorylated in a cell-cycle-dependent manner at serine or threonine residues in the SeriThr-Pro-Xaa-Lys and analogous amino acid sequences [11] level of H3 phosphorylation occurring at the 10th serine residue [16, 171 is evident only in M phase [18, 191 or during premature chromosome condensation [20, 211. We earlier indicated that H3 phosphorylation is specific to premature chromosome condensation since (a) H3 is dephosphorylated when the condensation is reversed without dephosphorylation of H1 [...

show abstract

Occurrence and properties of a chromatin-associated Fl-histone phosphokinase in mitotic Chinese hamster cells

Cited by 141 publications

References 29 publications

Absence of histone F1 in a mitotically dividing, genetically inactive nucleus.

Absence of histone F1 in a mitotically dividing, genetically inactive nucleus.

Activating Transcription Factor 3, a Stress-inducible Gene, Suppresses Ras-stimulated Tumorigenesis

Vanadate Triggers the Transition from Chromosome Condensation to Decondensation in a Mitotic Mutant (tsTM13)

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