Histone phosphorylation in late interphase and mitosis

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

doi:10.1016/0006-291x(73)91307-7

Cited by 84 publications

(42 citation statements)

References 14 publications

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“…It is readily apparent that fl and f2a2 were phosphorylated in these Colcemid-treated interphase cells, while histone f3 and the slow-migrating fl subfraction were not. An essentially identical histone phosphorylation pattern was obtained in interphase cells not treated with Colcemid (13) . Therefore, it appears that the Colcemid treatment for 2 h used in these experiments had no adverse effects on histone phosphorylation and does not P04 were then removed, and metaphase cells were allowed to enter G1 for 2 h. Histones were then prepared and subjected to preparative electrophoresis .…”

Section: Histone Phosphorylation Related To Mitosissupporting

confidence: 65%

“…By combining the data in this report with results obtained previously (11)(12)(13), we may obtain a view of the relationship between histone phosphorylation and the CHO cell cycle . This relationship is illustrated in Fig .…”

Section: Discussionmentioning

confidence: 53%

“…• phosphorylated f3 and a subfraction of fl (13), in addition to phosphorylation of fl and f2a2 normally seen in interphase cells (I1-13) . Lake…”

Section: Histone Phosphorylation Related To Mitosismentioning

confidence: 93%

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Cell Cycle-Specific Changes in Histone Phosphorylation Associated With Cell Proliferation and Chromosome Condensation

Gurley

Walters

Tobey

1974

The Journal of Cell Biology

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221

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Preparative polyacrylamide gel electrophoresis was used to examine histone phosphorylation in synchronized Chinese hamster cells (line CHO) . Results showed that histone fl phosphorylation, absent in GI-arrested and early GI-traversing cells, commences 2 h before entry of traversing cells into the S phase . It is concluded that fl phosphorylation is one of the earliest biochemical events associated with conversion of nonproliferating cells to proliferating cells occurring on old fi before synthesis of new fl during the S phase . Results also showed that f3 and a subfraction of fl were rapidly phosphorylated only during the time when cells were crossing the G 2/M boundary and traversing prophase .Since these phosphorylation events do not occur in G I , S, or G 2 and are reduced greatly in metaphase, it is concluded that these two specific phosphorylation events are involved with condensation of interphase chromatin into mitotic chromosomes . This conclusion is supported by loss of prelabeled 32 P04 from those specific histone fractions during transition of metaphase cells into interphase G, cells . A model of the relationship of histone phosphorylation to the cell cycle is presented which suggests involvement of fi phosphorylation in chromatin structural changes associated with a continuous interphase "chromosome cycle" which culminates at mitosis with an f3 and fl phosphorylation-mediated chromosome condensation .

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Section: Histone Phosphorylation Related To Mitosissupporting

confidence: 65%

Section: Discussionmentioning

confidence: 53%

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Cell Cycle-Specific Changes in Histone Phosphorylation Associated With Cell Proliferation and Chromosome Condensation

Gurley

Walters

Tobey

1974

The Journal of Cell Biology

Self Cite

221

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“…Histones are subject to a wide range of post-translational modifications throughout the cell cycle including phosphorylation, acetylation, and methylation (26). Histone H3 phosphorylation was first identified in mitotic cells and has since been recognized as a ubiquitous mitotic modification (2,3,60). However, phosphorylation of H3 Ser 10 also occurs in more discrete chromatin regions during activation of transcription and coincides with histone H3 acetylation on the same nucleosomes (61)(62)(63).…”

Section: Fig 4 Pp1 Regulates the Chromosome-associated Kinasementioning

confidence: 99%

Chromatin-associated Protein Phosphatase 1 Regulates Aurora-B and Histone H3 Phosphorylation

Murnion¹,

Adams²,

Callister³

et al. 2001

Journal of Biological Chemistry

229

192

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Proper chromosome condensation requires the phosphorylation of histone and nonhistone chromatin proteins. We have used an in vitro chromosome assembly system based on Xenopus egg cytoplasmic extracts to study mitotic histone H3 phosphorylation. We identified a histone H3 Ser 10 kinase activity associated with isolated mitotic chromosomes. The histone H3 kinase was not affected by inhibitors of cyclin-dependent kinases, DNA-dependent protein kinase, p90 rsk , or cAMP-dependent protein kinase. The activity could be selectively eluted from mitotic chromosomes and immunoprecipitated by specific anti-X aurora-B/AIRK2 antibodies. This activity was regulated by phosphorylation. Treatment of X aurora-B immunoprecipitates with recombinant protein phosphatase 1 (PP1) inhibited kinase activity. The presence of PP1 on chromatin suggested that PP1 might directly regulate the X aurora-B associated kinase activity. Indeed, incubation of isolated interphase chromatin with the PP1-specific inhibitor I2 and ATP generated an H3 kinase activity that was also specifically immunoprecipitated by anti-X aurora-B antibodies. Nonetheless, we found that stimulation of histone H3 phosphorylation in interphase cytosol does not drive chromosome condensation or targeting of 13 S condensin to chromatin. In summary, the chromosome-associated mitotic histone H3 Ser 10 kinase is associated with X aurora-B and is inhibited directly in interphase chromatin by PP1.

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“…Most studies have been done to relate histone phosphorylation with chromatin changes that occur during the cell-cycle, particularly involving chromatin condensation in mitosis (reviews: 3,4). Phosphorylation of histone H1 during entrance of cell to mitosis was reported over three decades ago (5), and the role of this modification in chromatin condensation has been postulated (6). More recent studies, however, have shown that histone H1 is not required for chromatin to undergo mitotic condensation (7,8).…”

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confidence: 99%

Sequential phosphorylation of Ser‐10 on histone H3 and ser‐139 on histone H2AX and ATM activation during premature chromosome condensation: Relationship to cell‐cycle phase and apoptosis

et al. 2006

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Background: Histone H1 and H3 phosphorylation associated with chromatin condensation during mitosis has been studied extensively. Less is known on histone modifications that occur during premature chromosome condensation (PCC). The aim of the present study was to reveal the status of histone H3 and H2AX phosphorylation on Ser-10 and Ser-139, respectively, as well as ATM activation through phosphorylation on Ser-1981, during PCC, and relate these events to cell-cycle phase and to initiation of apoptosis. Materials and Methods: To induce PCC, A549 and HL-60 cells were exposed to the phosphatase inhibitor calyculin A (Cal A). Phosphorylation of histone H3 and H2AX as well as ATM activation were detected immunocytochemically concurrent with analysis of cellular DNA content and activation of caspase-3, a marker of apoptosis. The intensity of cellular fluorescence was measured by flow-or laser scanning cytometry. Results: Induction of PCC led to rapid histone H3 phosphorylation, followed by activation of ATM and then H2AX

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Histone phosphorylation in late interphase and mitosis

Cited by 84 publications

References 14 publications

Cell Cycle-Specific Changes in Histone Phosphorylation Associated With Cell Proliferation and Chromosome Condensation

Cell Cycle-Specific Changes in Histone Phosphorylation Associated With Cell Proliferation and Chromosome Condensation

Chromatin-associated Protein Phosphatase 1 Regulates Aurora-B and Histone H3 Phosphorylation

Sequential phosphorylation of Ser‐10 on histone H3 and ser‐139 on histone H2AX and ATM activation during premature chromosome condensation: Relationship to cell‐cycle phase and apoptosis

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