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Beenders, Brent; Watrin, Erwan; Legagneux, Vincent; Kireev, Igor I.; Bellini, Michel

doi:10.1023/a:1024999316867

Cited by 13 publications

(5 citation statements)

References 45 publications

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“…This nucleolar localization of CAP-H, and also of CAP-C and CAP-E, has been previously described in interphase human HeLa cells ([30]). Likewise, some condensin I and II subunits have been found at nucleoli in interphase Xenopus ([41]), Arabidopsis and tobacco cultured cells ([40]), and also in Xenopus oocytes ([42]). It has been suggested that in higher eukaryotes the condensin complex may participate in the chromatin remodeling and condensation-dependent silencing of rDNA loci ([30]).…”

Section: Discussionmentioning

confidence: 99%

Condensin I Reveals New Insights on Mouse Meiotic Chromosome Structure and Dynamics

et al. 2007

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Chromosome shaping and individualization are necessary requisites to warrant the correct segregation of genomes in either mitotic or meiotic cell divisions. These processes are mainly prompted in vertebrates by three multiprotein complexes termed cohesin and condensin I and II. In the present study we have analyzed by immunostaining the appearance and subcellular distribution of condensin I in mouse mitotic and meiotic chromosomes. Our results demonstrate that in either mitotically or meiotically dividing cells, condensin I is loaded onto chromosomes by prometaphase. Condensin I is detectable as a fuzzy axial structure running inside chromatids of condensed chromosomes. The distribution of condensin I along the chromosome length is not uniform, since it preferentially accumulates close to the chromosome ends. Interestingly, these round accumulations found at the condensin I axes termini colocalized with telomere complexes. Additionally, we present the relative distribution of the condensin I and cohesin complexes in metaphase I bivalents. All these new data have allowed us to propose a comprehensive model for meiotic chromosome structure.

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Section: Discussionmentioning

confidence: 99%

Condensin I Reveals New Insights on Mouse Meiotic Chromosome Structure and Dynamics

et al. 2007

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“…Although in many species condensin localizes to the chromosome axis during mitotic cell division, it is also seen to accumulate at specific chromosome regions (Hirano and Mitchison, 1994; Steen et al ., 2000; Steffensen et al ., 2001; Beenders et al ., 2003; Savvidou et al ., 2005; Cuylen and Haering, 2011). In budding yeast, condensin is concentrated at rDNA throughout mitosis, becoming further enriched onto the rDNA at the start of anaphase, where it has a role in the organization and segregation of the rDNA (Freeman et al ., 2000; Bhalla et al ., 2002; Lavoie et al ., 2002; Yu and Koshland, 2003, 2005; D'Amours et al ., 2004; Machin et al ., 2004; Sullivan et al ., 2004; Wang et al ., 2004; Wang et al ., 2005; D'Ambrosio et al ., 2008a; Nakazawa et al ., 2008).…”

Section: Introductionmentioning

confidence: 99%

The condensin complexes play distinct roles to ensure normal chromosome morphogenesis during meiotic division in Arabidopsis

2014

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Meiosis is a specialized cell division essential for sexual reproduction. During meiosis the chromosomes are highly organized, and correct chromosome architecture is required for faithful segregation of chromosomes at anaphase I and II. Condensin is involved in chromosome organization during meiotic and mitotic cell divisions. Three condensin subunits, AtSMC4 and the condensin I and II specific subunits AtCAP-D2 and AtCAP-D3, respectively, have been studied for their role in meiosis. This has revealed that both the condensin I and condensin II complexes are required to maintain normal structural integrity of the meiotic chromosomes during the two nuclear divisions. Their roles appear functionally distinct in that condensin I is required to maintain normal compaction of the centromeric repeats and 45S rDNA, whereas loss of condensin II was associated with extensive interchromosome connections at metaphase I. Depletion of condensin is also associated with a slight reduction in crossover formation, suggesting a role during meiotic prophase I.

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“…However, lampbrush chromatin also appears distinctive with respect to the absence of typical chromatin components such as topoisomerase II (Hock et al 1996), HMGN proteins (Korner et al 2003) and condensin subunits (Beenders et al 2003). Particularly intriguing is the apparent absence from lampbrush chromatin of H1 linker histones (Hock et al 1993), given the many and varied roles that linker histones have in the structure and function of chromatin (Bustin et al 2005).…”

Section: Introductionmentioning

confidence: 99%

Association of modified cytosines and the methylated DNA-binding protein MeCP2 with distinctive structural domains of lampbrush chromatin

2012

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We have investigated the association of DNA methylation and proteins interpreting methylation state with the distinctive closed and open chromatin structural domains that are directly observable in the lampbrush chromosomes (LBCs) of amphibian oocytes. To establish the distribution in LBCs of MeCP2, one of the key proteins binding 5-methylcytosine-modified DNA (5mC), we expressed HA-tagged MeCP2 constructs in Xenopus laevis oocytes. Full-length MeCP2 was predominantly targeted to the closed, transcriptionally inactive chromomere domains in a pattern proportional to chromomeric DNA density and consistent with a global role in determining chromatin state. A minor fraction of HA-MeCP2 was also found to associate with a distinctive structural domain, namely a short region at the bases of some of the extended lateral loops. Expression in oocytes of deleted constructs and of point mutants derived from Rett syndrome patients demonstrated that the association of MeCP2 with LBCs was determined by its 5mC-binding domain. We also examined more directly the distribution of 5mC by immunostaining Xenopus and axolotl LBCs and confirmed the pattern suggested by MeCP2 targeting of intense staining of the chromomeres and of some loop bases. In addition, we found in the longer loops of axolotl LBCs that short interstitial regions could also be clearly stained for 5mC. These 5mC regions corresponded precisely to unusual segments of active transcription units from which RNA polymerase II (pol II) and nascent transcripts were simultaneously absent. We also examined by immunostaining the distribution in lampbrush chromatin of the oxidized 5mC derivative, 5-hydroxymethylcytosine (5hmC). Although in general, the pattern resembled that obtained for 5mC, one antibody against 5hmC produced intense staining of restricted chromosomal foci. These foci corresponded to a third type of lampbrush chromatin domain, the transcriptionally active but less extended structures formed by clusters of genes transcribed by pol III. This raises the possibility that 5hmC may play a role in establishing the distinctive patterns of gene repression and activation that characterize specific pol III-transcribed gene families in amphibian genomes.

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Cited by 13 publications

References 45 publications

Condensin I Reveals New Insights on Mouse Meiotic Chromosome Structure and Dynamics

Condensin I Reveals New Insights on Mouse Meiotic Chromosome Structure and Dynamics

The condensin complexes play distinct roles to ensure normal chromosome morphogenesis during meiotic division in Arabidopsis

Association of modified cytosines and the methylated DNA-binding protein MeCP2 with distinctive structural domains of lampbrush chromatin

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