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.

scholarly journals Phosphorylation-induced Rearrangement of the Histone H3 NH2-terminal Domain during Mitotic Chromosome Condensation

1999 ◽  
Vol 145 (2) ◽  
pp. 225-235 ◽  
Author(s):  
Debra M. Sauvé ◽  
Hilary J. Anderson ◽  
Jill M. Ray ◽  
William M. James ◽  
Michel Roberge
Keyword(s):  
Mitotic Chromosome ◽  
Kinase Inhibitor ◽  
Histone H3 ◽  
Chromosome Condensation ◽  
Early Prophase ◽  
Terminal Domain ◽  
Mitotic Chromosome Condensation ◽  
Chromosome Decondensation ◽  
Mitotic Cells

The NH2-terminal domain (N-tail) of histone H3 has been implicated in chromatin compaction and its phosphorylation at Ser10 is tightly correlated with mitotic chromosome condensation. We have developed one mAb that specifically recognizes histone H3 N-tails phosphorylated at Ser10 (H3P Ab) and another that recognizes phosphorylated and unphosphorylated H3 N-tails equally well (H3 Ab). Immunocytochemistry with the H3P Ab shows that Ser10 phosphorylation begins in early prophase, peaks before metaphase, and decreases during anaphase and telophase. Unexpectedly, the H3 Ab shows stronger immunofluorescence in mitosis than interphase, indicating that the H3 N-tail is more accessible in condensed mitotic chromatin than in decondensed interphase chromatin. In vivo ultraviolet laser cross-linking indicates that the H3 N-tail is bound to DNA in interphase cells and that binding is reduced in mitotic cells. Treatment of mitotic cells with the protein kinase inhibitor staurosporine causes histone H3 dephosphorylation and chromosome decondensation. It also decreases the accessibility of the H3 N-tail to H3 Ab and increases the binding of the N-tail to DNA. These results indicate that a phosphorylation-dependent weakening of the association between the H3 N-tail and DNA plays a role in mitotic chromosome condensation.

scholarly journals Mps1 phosphorylation of condensin II controls chromosome condensation at the onset of mitosis

2014 ◽  
Vol 205 (6) ◽  
pp. 781-790 ◽  
Author(s):  
Yuya Kagami ◽  
Keishi Nihira ◽  
Shota Wada ◽  
Masaya Ono ◽  
Mariko Honda ◽  
...  
Keyword(s):  
Chromosome Segregation ◽  
Cell Cycle Progression ◽  
Mitotic Chromosome ◽  
Early Stage ◽  
Chromosome Condensation ◽  
Cycle Progression ◽  
Daughter Cells ◽  
Phosphorylation Event ◽  
G2 Phase ◽  
Mitotic Chromosome Condensation

During mitosis, genomic DNA is condensed into chromosomes to promote its equal segregation into daughter cells. Chromosome condensation occurs during cell cycle progression from G2 phase to mitosis. Failure of chromosome compaction at prophase leads to subsequent misregulation of chromosomes. However, the molecular mechanism that controls the early phase of mitotic chromosome condensation is largely unknown. Here, we show that Mps1 regulates initial chromosome condensation during mitosis. We identify condensin II as a novel Mps1-associated protein. Mps1 phosphorylates one of the condensin II subunits, CAP-H2, at Ser492 during mitosis, and this phosphorylation event is required for the proper loading of condensin II on chromatin. Depletion of Mps1 inhibits chromosomal targeting of condensin II and accurate chromosome condensation during prophase. These findings demonstrate that Mps1 governs chromosomal organization during the early stage of mitosis to facilitate proper chromosome segregation.

Mitosis-specific phosphorylation of histone H3 initiates primarily within pericentromeric heterochromatin during G2 and spreads in an ordered fashion coincident with mitotic chromosome condensation

Chromosoma ◽  
1997 ◽  
Vol 106 (6) ◽  
pp. 348-360 ◽  
Author(s):  
Michael J. Hendzel ◽  
Yi Wei ◽  
Michael A. Mancini ◽  
Aaron Van Hooser ◽  
Tamara Ranalli ◽  
...  
Keyword(s):  
Mitotic Chromosome ◽  
Histone H3 ◽  
Chromosome Condensation ◽  
Pericentromeric Heterochromatin ◽  
Mitotic Chromosome Condensation

scholarly journals Topoisomerase IIα is essential for maintenance of mitotic chromosome structure

2020 ◽  
Vol 117 (22) ◽  
pp. 12131-12142 ◽  
Author(s):  
Christian F. Nielsen ◽  
Tao Zhang ◽  
Marin Barisic ◽  
Paul Kalitsis ◽  
Damien F. Hudson
Keyword(s):  
Cell Cycle ◽  
Chromosome Segregation ◽  
Mitotic Chromosome ◽  
Chromosome Structure ◽  
Chromatin Condensation ◽  
Chromosome Condensation ◽  
Mitotic Chromosomes ◽  
Topoisomerase Iiα ◽  
Mitotic Chromosome Condensation

Topoisomerase IIα (TOP2A) is a core component of mitotic chromosomes and important for establishing mitotic chromosome condensation. The primary roles of TOP2A in mitosis have been difficult to decipher due to its multiple functions across the cell cycle. To more precisely understand the role of TOP2A in mitosis, we used the auxin-inducible degron (AID) system to rapidly degrade the protein at different stages of the human cell cycle. Removal of TOP2A prior to mitosis does not affect prophase timing or the initiation of chromosome condensation. Instead, it prevents chromatin condensation in prometaphase, extends the length of prometaphase, and ultimately causes cells to exit mitosis without chromosome segregation occurring. Surprisingly, we find that removal of TOP2A from cells arrested in prometaphase or metaphase cause dramatic loss of compacted mitotic chromosome structure and conclude that TOP2A is crucial for maintenance of mitotic chromosomes. Treatments with drugs used to poison/inhibit TOP2A function, such as etoposide and ICRF-193, do not phenocopy the effects on chromosome structure of TOP2A degradation by AID. Our data point to a role for TOP2A as a structural chromosome maintenance enzyme locking in condensation states once sufficient compaction is achieved.

scholarly journals Axial contraction and short-range compaction of chromatin synergistically promote mitotic chromosome condensation

eLife ◽  
2015 ◽  
Vol 4 ◽  
Author(s):  
Tom Kruitwagen ◽  
Annina Denoth-Lippuner ◽  
Bryan J Wilkins ◽  
Heinz Neumann ◽  
Yves Barral
Keyword(s):  
Short Range ◽  
Mitotic Chromosome ◽  
Chromosome Condensation ◽  
Yeast Cells ◽  
Histone H4 ◽  
Mitotic Chromosomes ◽  
Chromatin Compaction ◽  
Early Anaphase ◽  
Local Compaction ◽  
Mitotic Chromosome Condensation

The segregation of eukaryotic chromosomes during mitosis requires their extensive folding into units of manageable size for the mitotic spindle. Here, we report on how phosphorylation at serine 10 of histone H3 (H3 S10) contributes to this process. Using a fluorescence-based assay to study local compaction of the chromatin fiber in living yeast cells, we show that chromosome condensation entails two temporally and mechanistically distinct processes. Initially, nucleosome-nucleosome interaction triggered by H3 S10 phosphorylation and deacetylation of histone H4 promote short-range compaction of chromatin during early anaphase. Independently, condensin mediates the axial contraction of chromosome arms, a process peaking later in anaphase. Whereas defects in chromatin compaction have no observable effect on axial contraction and condensin inactivation does not affect short-range chromatin compaction, inactivation of both pathways causes synergistic defects in chromosome segregation and cell viability. Furthermore, both pathways rely at least partially on the deacetylase Hst2, suggesting that this protein helps coordinating chromatin compaction and axial contraction to properly shape mitotic chromosomes.

Aurora-B phosphorylates Histone H3 at serine28 with regard to the mitotic chromosome condensation

2002 ◽  
Vol 7 (1) ◽  
pp. 11-17 ◽  
Author(s):  
Hidemasa Goto ◽  
Yoshihiro Yasui ◽  
Erich A. Nigg ◽  
Masaki Inagaki
Keyword(s):  
Mitotic Chromosome ◽  
Histone H3 ◽  
Chromosome Condensation ◽  
Aurora B ◽  
Mitotic Chromosome Condensation

scholarly journals In vivo dissection of the chromosome condensation machinery

2002 ◽  
Vol 156 (5) ◽  
pp. 805-815 ◽  
Author(s):  
Brigitte D. Lavoie ◽  
Eileen Hogan ◽  
Douglas Koshland
Keyword(s):  
Topoisomerase Ii ◽  
Mitotic Chromosome ◽  
Chromosome Structure ◽  
Histone H3 ◽  
Chromosome Condensation ◽  
Chromatin Binding ◽  
Condensin Complex ◽  
Topo Ii ◽  
Structural Maintenance Of Chromosome

The machinery mediating chromosome condensation is poorly understood. To begin to dissect the in vivo function(s) of individual components, we monitored mitotic chromosome structure in mutants of condensin, cohesin, histone H3, and topoisomerase II (topo II). In budding yeast, both condensation establishment and maintenance require all of the condensin subunits, but not topo II activity or phospho-histone H3. Structural maintenance of chromosome (SMC) protein 2, as well as each of the three non-SMC proteins (Ycg1p, Ycs4p, and Brn1p), was required for chromatin binding of the condensin complex in vivo. Using reversible condensin alleles, we show that chromosome condensation does not involve an irreversible modification of condensin or chromosomes. Finally, we provide the first evidence of a mechanistic link between condensin and cohesin function. A model discussing the functional interplay between cohesin and condensin is presented.

scholarly journals Chromosome Condensation Factor Brn1p Is Required for Chromatid Separation in Mitosis

2000 ◽  
Vol 11 (4) ◽  
pp. 1305-1313 ◽  
Author(s):  
Ilia I. Ouspenski ◽  
Olga A. Cabello ◽  
B. R. Brinkley
Keyword(s):  
Chromosome Segregation ◽  
Mitotic Chromosome ◽  
Nuclear Protein ◽  
Chromosome Condensation ◽  
Temperature Sensitive ◽  
Condensin Complex ◽  
Chromatid Cohesion ◽  
Protein Functions ◽  
Mitotic Chromosome Condensation ◽  
Mutant Cells

This work describes BRN1, the budding yeast homologue of Drosophila Barren andXenopus condensin subunit XCAP-H. TheDrosophila protein is required for proper chromosome segregation in mitosis, and Xenopus protein functions in mitotic chromosome condensation. Mutant brn1 cells show a defect in mitotic chromosome condensation and sister chromatid separation and segregation in anaphase. Chromatid cohesion before anaphase is properly maintained in the mutants. Somebrn1 mutant cells apparently arrest in S-phase, pointing to a possible function for Brn1p at this stage of the cell cycle. Brn1p is a nuclear protein with a nonuniform distribution pattern, and its level is up-regulated at mitosis. Temperature-sensitive mutations ofBRN1 can be suppressed by overexpression of a novel geneYCG1, which is homologous to anotherXenopus condensin subunit, XCAP-G. Overexpression ofSMC2, a gene necessary for chromosome condensation, and a homologue of the XCAP-E condensin, does not suppress brn1, pointing to functional specialization of components of the condensin complex.

scholarly journals Identification of a Novel Phosphorylation Site on Histone H3 Coupled with Mitotic Chromosome Condensation

1999 ◽  
Vol 274 (36) ◽  
pp. 25543-25549 ◽  
Author(s):  
Hidemasa Goto ◽  
Yasuko Tomono ◽  
Kozo Ajiro ◽  
Hidetaka Kosako ◽  
Masatoshi Fujita ◽  
...  
Keyword(s):  
Mitotic Chromosome ◽  
Phosphorylation Site ◽  
Histone H3 ◽  
Chromosome Condensation ◽  
Mitotic Chromosome Condensation

scholarly journals Condensins under the microscope

2018 ◽  
Vol 217 (7) ◽  
pp. 2229-2231 ◽  
Author(s):  
Kazuhiro Maeshima ◽  
Kayo Hibino ◽  
Damien F. Hudson
Keyword(s):  
Quantitative Data ◽  
Mitotic Chromosome ◽  
State Of The Art ◽  
Imaging Techniques ◽  
Mechanistic Model ◽  
Chromosome Condensation ◽  
Mitotic Chromosomes ◽  
Cell Biol ◽  
Key Players ◽  
Mitotic Chromosome Condensation

Condensins are key players in mitotic chromosome condensation. Using an elegant combination of state-of-the-art imaging techniques, Walther et al. (2018. J. Cell Biol. https://doi.org/10.1083/jcb.201801048) counted the number of Condensins, examined their behaviors on human mitotic chromosomes, and integrated the quantitative data to propose a new mechanistic model for chromosome condensation.

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