Meiotic events at the centromeric heterochromatin: histone H3 phosphorylation, topoisomerase IIα localization and chromosome condensation

Chromosoma ◽  
1999 ◽  
Vol 108 (7) ◽  
pp. 412-425 ◽  
Author(s):  
John Cobb ◽  
Mitsuko Miyaike ◽  
Akihiko Kikuchi ◽  
Mary Ann Handel
Keyword(s):  
Histone H3 ◽  
Chromosome Condensation ◽  
Centromeric Heterochromatin ◽  
Topoisomerase Iiα ◽  
H3 Phosphorylation ◽  
Histone H3 Phosphorylation

scholarly journals Cell Cycle-dependent Expression and Nucleolar Localization of hCAP-H

2001 ◽  
Vol 12 (11) ◽  
pp. 3527-3537 ◽  
Author(s):  
Olga A. Cabello ◽  
Elena Eliseeva ◽  
WeiGong He ◽  
Hagop Youssoufian ◽  
Sharon E. Plon ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Histone H3 ◽  
Chromosome Condensation ◽  
Nucleolar Localization ◽  
Mitotic Chromosomes ◽  
Proliferating Cells ◽  
Protein Levels ◽  
Sister Chromatids ◽  
H3 Phosphorylation ◽  
Histone H3 Phosphorylation

Condensin is a conserved 13S heteropentamer composed of two nonidentical structural maintenance of chromosome (SMC) family proteins, in Xenopus XCAP-C and XCAP-E, and three regulatory subunits, XCAP-D2, XCAP-G, and XCAP-H. Both biochemical and genetic analyses have demonstrated an essential role for the 13S condensin complex in mitotic chromosome condensation. Further, a potential requirement for condensin in completion of chromatid arm separation in early anaphase is demonstrated by the mutational phenotypes of the Drosophila homologues ofXCAP-H, barren and XCAP-C,DmSMC4. In this study we have investigated the expression and subcellular distribution of hCAP-H, the human homolog of XCAP-H, in order to better understand its cellular functions. Transcription of hCAP-H was restricted to proliferating cells with highest expression during the G2 phase of the cell cycle. In contrast, cellular hCAP-H protein levels were constant throughout the cell cycle. hCAP-H was found to be associated with mitotic chromosomes exhibiting a nonuniform but symmetric distribution along sister chromatids. The symmetry of hCAP-H association with sister chromatids suggests that there are sequence-dependent domains of condensin aggregation. During interphase hCAP-H, -C, and -E, have distinct punctate nucleolar localization, suggesting that condensin may associate with and modulate the conformation and function of rDNA. hCAP-H association with condensed chromatin was not observed in the early phase of chromosome condensation when histone H3 phosphorylation has already taken place. This finding is consistent with the hypothesis that histone H3 phosphorylation precedes condensin-mediated condensation.

scholarly journals Drosophila Aurora B Kinase Is Required for Histone H3 Phosphorylation and Condensin Recruitment during Chromosome Condensation and to Organize the Central Spindle during Cytokinesis

2001 ◽  
Vol 152 (4) ◽  
pp. 669-682 ◽  
Author(s):  
Régis Giet ◽  
David M. Glover
Keyword(s):  
Histone H3 ◽  
Chromosome Condensation ◽  
Aurora B ◽  
Aurora B Kinase ◽  
Kinase Gene ◽  
Central Spindle ◽  
H3 Phosphorylation ◽  
Founding Family ◽  
Reduced Density ◽  
Histone H3 Phosphorylation

Aurora/Ipl1-related kinases are a conserved family of enzymes that have multiple functions during mitotic progression. Although it has been possible to use conventional genetic analysis to dissect the function of aurora, the founding family member in Drosophila (Glover, D.M., M.H. Leibowitz, D.A. McLean, and H. Parry. 1995. Cell. 81:95–105), the lack of mutations in a second aurora-like kinase gene, aurora B, precluded this approach. We now show that depleting Aurora B kinase using double-stranded RNA interference in cultured Drosophila cells results in polyploidy. aurora B encodes a passenger protein that associates first with condensing chromatin, concentrates at centromeres, and then relocates onto the central spindle at anaphase. Cells depleted of the Aurora B kinase show only partial chromosome condensation at mitosis. This is associated with a reduction in levels of the serine 10 phosphorylated form of histone H3 and a failure to recruit the Barren condensin protein onto chromosomes. These defects are associated with abnormal segregation resulting from lagging chromatids and extensive chromatin bridging at anaphase, similar to the phenotype of barren mutants (Bhat, M.A., A.V. Philp, D.M. Glover, and H.J. Bellen. 1996. Cell. 87:1103–1114.). The majority of treated cells also fail to undertake cytokinesis and show a reduced density of microtubules in the central region of the spindle. This is accompanied by a failure to correctly localize the Pavarotti kinesin-like protein, essential for this process. We discuss these conserved functions of Aurora B kinase in chromosome transmission and cytokinesis.

scholarly journals 309CHROMOSOME CONDENSATION IS CORRELATED WITH HISTONE H3 PHOSPHORYLATION WITHOUT CDC2 KINASE AND MAP KINASE ACTIVITIES IN PIG OOCYTES

2004 ◽  
Vol 16 (2) ◽  
pp. 273
Author(s):  
T. Bui Hong ◽  
L.G. Villa-Diaz ◽  
E. Yamaoka ◽  
T. Miyano
Keyword(s):  
Map Kinase ◽  
Kinase Activity ◽  
Histone H3 ◽  
Germinal Vesicle ◽  
Chromosome Condensation ◽  
Kinase Assay ◽  
Cdc2 Kinase ◽  
H3 Phosphorylation ◽  
Diakinesis Stage ◽  
Histone H3 Phosphorylation

Chromosome condensation is the first step of oocyte maturation. When the oocytes resume meiosis, chromosomes start to condense and Cdc2 kinase becomes activated. However, recent findings show that the chromosome condensation does not always correlate with Cdc2 kinase activity in pig oocytes. The objectives of this study were to examine (1) the correlation between chromosome condensation and histone H3 phosphorylation at serine 10 (Ser10) during meiotic maturation of pig oocytes, and (2) the effects of protein phosphatase 1/2A (PP1/PP2A) inhibitors on the chromosome condensation and the involvement of Cdc2 kinase, MAP kinase and histone H3 kinase in this process. Oocyte-cumulus-granulosa cell complexes (OCGCs) were collected from follicles of 4–6mm in diameter. OCGCs were cultured in modified TCM 199 for different periods of time to obtain oocytes at the germinal vesicle (GV, 0h), diakinesis (18h), metaphase I (24–27h), anaphase I to telophase I (30–33h), and metaphase II (42h) stages. To examine the effects of PP1/PP2A inhibitors on the chromosome condensation, oocyte-cumulus-complexes (OCCs) were cultured in modified TCM 199 with either 2.5μM okadaic acid (OA) or 50nM calyculin A (CL-A) for 0.5, 1, 2, 3, 4 and 6h. To inhibit the MAP kinase activity in the oocytes treated with the PP1/PP2A inhibitor, OCCs were cultured in medium containing CL-A and the MEK inhibitor, U0126 (0.1mM). Morphology of the chromosome and nuclear membrane, and phosphorylation of histone H3 were examined by the immunofluorescent microscopy. In each group 30 oocytes were examined for OA or CL-A and 60 oocytes for CL-A+U0126 treatments. Activities of Cdc2 kinase, MAP kinase and histone H3 kinase were also examined. Phosphorylation of histone H3 (Ser10) was not detected in the oocytes at the GV stage. The phosphorylation was first detected in the clump of condensed chromosomes at the diakinesis stage of prophase I and maintained until metaphase II. The kinase assay also showed that histone H3 kinase activity was low in GV oocytes, increased at the diakinesis stage, and then maintained high activity until metaphase II. PP1/PP2A inhibitors induced rapid chromosome condensation in pig oocytes. Histone H3 phosphorylation (Ser10) became detectable together with the chromosome condensation in the treated oocytes after 2h. After 6h, oocytes had highly condensed chromosomes with phosphorylated histone H3 (81% in CL-A- and 71% in OA-treated oocytes). Both histone H3 kinase and MAP kinase were activated in the treated oocytes, although Cdc2 kinase was not activated. In the oocytes treated with CL-A and U0126, neither Cdc2 kinase nor MAP kinase were activated, although histone H3 kinase was still activated and chromosomes condensed. These results suggest that phosphorylation of histone H3 (Ser10) occurs in condensed chromosomes during maturation in pig oocytes. Futhermore, the chromosome condensation is correlated with histone H3 kinase activity, but not with Cdc2 kinase and MAP kinase activities.

Histone H3 phosphorylation is required for the initiation, but not maintenance, of mammalian chromosome condensation

1998 ◽  
Vol 111 (23) ◽  
pp. 3497-3506 ◽  
Author(s):  
A. Van Hooser ◽  
D.W. Goodrich ◽  
C.D. Allis ◽  
B.R. Brinkley ◽  
M.A. Mancini
Keyword(s):  
Cell Cycle Progression ◽  
Histone H3 ◽  
Chromosome Morphology ◽  
Chromosome Condensation ◽  
S Phase ◽  
Condensed State ◽  
Cycle Progression ◽  
H3 Phosphorylation ◽  
Excess Substrate ◽  
Histone H3 Phosphorylation

The temporal and spatial patterns of histone H3 phosphorylation implicate a specific role for this modification in mammalian chromosome condensation. Cells arrest in late G2 when H3 phosphorylation is competitively inhibited by microinjecting excess substrate at mid-S-phase, suggesting a requirement for activity of the kinase that phosphorylates H3 during the initiation of chromosome condensation and entry into mitosis. Basal levels of phosphorylated H3 increase primarily in late-replicating/early-condensing heterochromatin both during G2 and when premature chromosome condensation is induced. The prematurely condensed state induced by okadaic acid treatment during S-phase culminates with H3 phosphorylation throughout the chromatin, but in an absence of mitotic chromosome morphology, indicating that the phosphorylation of H3 is not sufficient for complete condensation. Mild hypotonic treatment of cells arrested in mitosis results in the dephosphorylation of H3 without a cytological loss of chromosome compaction. Hypotonic-treated cells, however, complete mitosis only when H3 is phosphorylated. These observations suggest that H3 phosphorylation is required for cell cycle progression and specifically for the changes in chromatin structure incurred during chromosome condensation.

scholarly journals Chromatin remodeling in somatic cells injected into mature pig oocytes

Reproduction ◽  
2006 ◽  
Vol 131 (6) ◽  
pp. 1037-1049 ◽  
Author(s):  
Hong-Thuy Bui ◽  
Nguyen Van Thuan ◽  
Teruhiko Wakayama ◽  
Takashi Miyano
Keyword(s):  
Somatic Cell ◽  
Somatic Cells ◽  
Histone H3 ◽  
Chromosome Morphology ◽  
Chromosome Condensation ◽  
Cell Nuclei ◽  
H3 Phosphorylation ◽  
Histone H3 Methylation ◽  
Histone H3 Phosphorylation

We examined the involvement of histone H3 modifications in the chromosome condensation and decondensation of somatic cell nuclei injected into mature pig oocytes. Nuclei of pig granulosa cells were transferred into in vitro matured intact pig oocytes, and histone H3 phosphorylation, acetylation, and methylation were examined by immunostaining with specific antibodies in relation to changes in chromosome morphology. In the condensed chromosomes of pig oocytes at metaphase II, histone H3 was phosphorylated at serine 10 (H3–S10) and serine 28 (H3–S28), and methylated at lysine 9 (H3–K9), but was not acetylated at lysine 9, 14 and 18 (H3–K9, H3–K14 and H3–K18). During the first 2 h after nuclear transfer, a series of events were observed in the somatic nuclei: nuclear membrane disassembly; chromosome condensation to form a metaphase-like configuration; an increase in histone H3 phosphorylation levels (H3–S10 and H3–S28). Next, pig oocytes injected with nuclei of somatic cells were electroactivated and the chromosome morphology of oocytes and somatic cells was examined along with histone modifications. Generally, chromosomes of the somatic cells showed a similar progression of cell cycle stage to that of oocytes, through anaphase II- and telophase II-like stages then formed pronucleus-like structures, although the morphology of the spindles differed from that of oocyte spindles. The chromosomes of somatic cells also showed changes in histone H3 dephosphorylation and reacetylation, similar to oocytes. In contrast, histone H3 methylation (H3–K9) of somatic cell nuclei did not show any significant change after injection and electroactivation of the oocytes. These results suggest that nuclear remodeling including histone H3 phosphorylation and acetylation of injected somatic nuclei took place in the oocytes under regulation by the oocyte cytoplasm.

N-Acetyl-chitobiose ameliorates metabolism dysfunction through Erk/p38 MAPK and histone H3 phosphorylation in type 2 diabetes mice

2017 ◽  
Vol 28 ◽  
pp. 96-105 ◽  
Author(s):  
Xia Wu ◽  
Jing Wang ◽  
Yuqin Shi ◽  
Sai Chen ◽  
Qiaojuan Yan ◽  
...  
Keyword(s):  
Type 2 Diabetes ◽  
P38 Mapk ◽  
Histone H3 ◽  
Diabetes Mice ◽  
H3 Phosphorylation ◽  
Histone H3 Phosphorylation
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