scholarly journals A phospho/methyl switch at histone H3 regulates TFIID association with mitotic chromosomes

2010 ◽  
Vol 29 (23) ◽  
pp. 3967-3978 ◽  
Author(s):  
Radhika A Varier ◽  
Nikolay S Outchkourov ◽  
Petra de Graaf ◽  
Frederik M A van Schaik ◽  
Henk Jan L Ensing ◽  
...  
Keyword(s):  
Histone H3 ◽  
Mitotic Chromosomes

scholarly journals Phosphorylation of Histone H3 at Serine 10 Cannot Account Directly for the Detachment of Human Heterochromatin Protein 1γ from Mitotic Chromosomes in Plant Cells

2002 ◽  
Vol 277 (34) ◽  
pp. 30921-30927 ◽  
Author(s):  
Ephraim Fass ◽  
Shai Shahar ◽  
Jing Zhao ◽  
Assaf Zemach ◽  
Yigal Avivi ◽  
...  
Keyword(s):  
Histone H3 ◽  
Plant Cells ◽  
Mitotic Chromosomes ◽  
Heterochromatin Protein

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 A Bromodomain Protein, MCAP, Associates with Mitotic Chromosomes and Affects G2-to-M Transition

2000 ◽  
Vol 20 (17) ◽  
pp. 6537-6549 ◽  
Author(s):  
Anup Dey ◽  
Jan Ellenberg ◽  
Andrea Farina ◽  
Allen E. Coleman ◽  
Tetsuo Maruyama ◽  
...  
Keyword(s):  
Mitotic Chromosome ◽  
Histone H3 ◽  
Growth Stimulation ◽  
Nuclear Factor ◽  
Cell Nuclei ◽  
Mitotic Chromosomes ◽  
H3 Phosphorylation ◽  
Chromosomal Condensation ◽  
Histone H3 Phosphorylation ◽  
Exquisite Specificity

ABSTRACT We describe a novel nuclear factor called mitotic chromosome-associated protein (MCAP), which belongs to the poorly understood BET subgroup of the bromodomain superfamily. Expression of the 200-kDa MCAP was linked to cell division, as it was induced by growth stimulation and repressed by growth inhibition. The most notable feature of MCAP was its association with chromosomes during mitosis, observed at a time when the majority of nuclear regulatory factors were released into the cytoplasm, coinciding with global cessation of transcription. Indicative of its predominant interaction with euchromatin, MCAP localized on mitotic chromosomes with exquisite specificity: (i) MCAP-chromosome association became evident subsequent to the initiation of histone H3 phosphorylation and early chromosomal condensation; and (ii) MCAP was absent from centromeres, the sites of heterochromatin. Supporting a role for MCAP in G2/M transition, microinjection of anti-MCAP antibody into HeLa cell nuclei completely inhibited the entry into mitosis, without abrogating the ongoing DNA replication. These results suggest that MCAP plays a role in a process governing chromosomal dynamics during mitosis.

The cell cycle dependent phosphorylation of histone H3 is correlated with the condensation of plant mitotic chromosomes

1999 ◽  
Vol 18 (6) ◽  
pp. 675-679 ◽  
Author(s):  
Andreas Houben ◽  
Toshiyuki Wako ◽  
Rieko Furushima-Shimogawara ◽  
Gernot Presting ◽  
Gottfried Kunzel ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Histone H3 ◽  
Mitotic Chromosomes ◽  
Cycle Dependent

scholarly journals Tripartite chromatin localization of budding yeast Shugoshin involves higher-ordered architecture of mitotic chromosomes

2018 ◽  
Author(s):  
Xiexiong Deng ◽  
Min-Hao Kuo
Keyword(s):  
Spindle Assembly Checkpoint ◽  
Mitotic Chromosome ◽  
Budding Yeast ◽  
Histone H3 ◽  
Spindle Assembly ◽  
Mitotic Spindles ◽  
Mitotic Chromosomes ◽  
Chromatin Architecture ◽  
Sister Chromatids ◽  
Segregation Of Chromosomes

ABSTRACTThe spindle assembly checkpoint (SAC) is key to faithful segregation of chromosomes. One requirement that satisfies SAC is appropriate tension between sister chromatids at the metaphase-anaphase juncture. Proper tension generated by poleward pulling of mitotic spindles signals biorientation of the underlying chromosome. In the budding yeast, the tension status is monitored by the conserved Shugoshin protein, Sgo1p, and the tension sensing motif (TSM) of histone H3. ChIP-seq reveals a unique TSM-dependent, tripartite domain of Sgo1p in each mitotic chromosome. This domain consists of one centromeric and two flanking peaks 3 – 4 kb away, and is present exclusively in mitosis. Strikingly, this trident motif coincides with cohesin localization, but only at the centromere and the two immediate adjacent loci, despite that cohesin is enriched at numerous regions throughout mitotic chromosomes. The TSM-Sgo1p-cohesin triad is at the center stage of higher-ordered chromatin architecture for error-free segregation.

scholarly journals A novel chromatin tether domain controls topoisomerase IIα dynamics and mitotic chromosome formation

2013 ◽  
Vol 203 (3) ◽  
pp. 471-486 ◽  
Author(s):  
Andrew B. Lane ◽  
Juan F. Giménez-Abián ◽  
Duncan J. Clarke
Keyword(s):  
Posttranslational Modifications ◽  
Mitotic Chromosome ◽  
Histone H3 ◽  
Important Class ◽  
Histone Tail ◽  
Mitotic Chromosomes ◽  
Topoisomerase Iiα ◽  
Dna Topoisomerase ◽  
Chromosome Formation ◽  
Dna Topoisomerase Iiα

DNA topoisomerase IIα (Topo IIα) is the target of an important class of anticancer drugs, but tumor cells can become resistant by reducing the association of the enzyme with chromosomes. Here we describe a critical mechanism of chromatin recruitment and exchange that relies on a novel chromatin tether (ChT) domain and mediates interaction with histone H3 and DNA. We show that the ChT domain controls the residence time of Topo IIα on chromatin in mitosis and is necessary for the formation of mitotic chromosomes. Our data suggest that the dynamics of Topo IIα on chromosomes are important for successful mitosis and implicate histone tail posttranslational modifications in regulating Topo IIα.

scholarly journals A Human Condensin Complex Containing hCAP-C–hCAP-E and CNAP1, a Homolog of Xenopus XCAP-D2, Colocalizes with Phosphorylated Histone H3 during the Early Stage of Mitotic Chromosome Condensation

2000 ◽  
Vol 20 (18) ◽  
pp. 6996-7006 ◽  
Author(s):  
John A. Schmiesing ◽  
Heather C. Gregson ◽  
Sharleen Zhou ◽  
Kyoko Yokomori
Keyword(s):  
Mammalian Cells ◽  
Structural Changes ◽  
Mitotic Chromosome ◽  
Early Stage ◽  
Histone H3 ◽  
Chromosome Condensation ◽  
Early Prophase ◽  
Mitotic Chromosomes ◽  
Condensin Complex ◽  
Mitotic Chromosome Condensation

ABSTRACT Structural maintenance of chromosomes (SMC) family proteins play critical roles in structural changes of chromosomes. Previously, we identified two human SMC family proteins, hCAP-C and hCAP-E, which form a heterodimeric complex (hCAP-C–hCAP-E) in the cell. Based on the sequence conservation and mitotic chromosome localization, hCAP-C–hCAP-E was determined to be the human ortholog of theXenopus SMC complex, XCAP-C–XCAP-E. XCAP-C–XCAP-E is a component of the multiprotein complex termed condensin, required for mitotic chromosome condensation in vitro. However, presence of such a complex has not been demonstrated in mammalian cells. Coimmunoprecipitation of the endogenous hCAP-C–hCAP-E complex from HeLa extracts identified a 155-kDa protein interacting with hCAP-C–hCAP-E, termed condensation-related SMC-associated protein 1 (CNAP1). CNAP1 associates with mitotic chromosomes and is homologous toXenopus condensin component XCAP-D2, indicating the presence of a condensin complex in human cells. Chromosome association of human condensin is mitosis specific, and the majority of condensin dissociates from chromosomes and is sequestered in the cytoplasm throughout interphase. However, a subpopulation of the complex was found to remain on chromosomes as foci in the interphase nucleus. During late G2/early prophase, the larger nuclear condensin foci colocalize with phosphorylated histone H3 clusters on partially condensed regions of chromosomes. These results suggest that mitosis-specific function of human condensin may be regulated by cell cycle-specific subcellular localization of the complex, and the nuclear condensin that associates with interphase chromosomes is involved in the reinitiation of mitotic chromosome condensation in conjunction with phosphorylation of histone H3.

Phosphorylation of histone H3 is correlated with changes in the maintenance of sister chromatid cohesion during meiosis in maize, rather than the condensation of the chromatin

2000 ◽  
Vol 113 (18) ◽  
pp. 3217-3226 ◽  
Author(s):  
E. Kaszas ◽  
W.Z. Cande
Keyword(s):  
Sister Chromatid ◽  
Meiotic Chromosome ◽  
Histone H3 ◽  
Sister Chromatid Cohesion ◽  
Chromosome Condensation ◽  
Mitotic Chromosomes ◽  
Sister Chromatids ◽  
H3 Phosphorylation ◽  
Chromatid Cohesion ◽  
Metaphase I

Meiotic chromosome condensation is a unique process, characterized by dramatic changes in chromosome morphology that are required for the correct progression of pairing, synapsis, recombination and segregation of sister chromatids. We used an antibody that recognizes a ser 10 phosphoepitope on histone H3 to monitor H3 phosphorylation during meiosis in maize meiocytes. H3 phosphorylation has been reported to be an excellent marker for chromosome condensation during mitotic prophase in animal cells. In this study, we find that on maize mitotic chromosomes only pericentromeric regions are stained; there is little staining on the arms. During meiosis, chromosome condensation from leptotene through diplotene occurs in the absence of H3 phosphorylation. Instead, the changes in H3 phosphorylation at different stages of meiosis correlate with the differences in requirements for sister chromatid cohesion at different stages. Just before nuclear envelope breakdown, histone H3 phosphorylation is seen first in the pericentromeric regions and then extends through the arms at metaphase I; at metaphase II only the pericentromeric regions are stained. In afd1 (absence of first division), a mutant that is defective in many aspects of meiosis including sister chromatid cohesion and has equational separation at metaphase I, staining is restricted to the pericentromeric regions during metaphase I and anaphase I; there is no staining at metaphase II or anaphase II. We conclude that changes in the level of phosphorylation of ser10 in H3 correspond to changes in the cohesion of sister chromatids rather than the extent of chromosome condensation at different stages of meiosis.

scholarly journals Chromatin Binding of SRp20 and ASF/SF2 and Dissociation from Mitotic Chromosomes Is Modulated by Histone H3 Serine 10 Phosphorylation

2009 ◽  
Vol 33 (4) ◽  
pp. 450-461 ◽  
Author(s):  
Rebecca J. Loomis ◽  
Yoshinori Naoe ◽  
J. Brandon Parker ◽  
Velibor Savic ◽  
Matthew R. Bozovsky ◽  
...  
Keyword(s):  
Histone H3 ◽  
Chromatin Binding ◽  
Mitotic Chromosomes
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