Contribution of hCAP-D2, a Non-SMC Subunit of Condensin I, to Chromosome and Chromosomal Protein Dynamics during Mitosis

Watrin, Erwan; Legagneux, Vincent

doi:10.1128/mcb.25.2.740-750.2005

Cited by 39 publications

(36 citation statements)

References 65 publications

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“…It has been reported that the Drosophila non-SMC condensin subunit Barren (CAP-H) interacts with Topo II, stimulating its activity (66). Consistent with this report, depletion of the Condensin I non-SMC subunit CAP-D2 leads to an alteration of the spatial organization of Topo II in both Drosophila and humans, along with a change in CAP-H levels or localization (67,68). Moreover, Topo II appears to be improperly localized in mitotic chromosomes from SMC-2 or SMC-4 depleted cell extracts (for a review, see ref.…”

Section: Discussionsupporting

confidence: 77%

Escherichia coli condensin MukB stimulates topoisomerase IV activity by a direct physical interaction

Stewart

Berger

et al. 2010

Proc. Natl. Acad. Sci. U.S.A.

139

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In contrast to the current state of knowledge in the field of eukaryotic chromosome segregation, relatively little is known about the mechanisms coordinating the appropriate segregation of bacterial chromosomes. In Escherichia coli , the MukB/E/F complex and topoisomerase IV (Topo IV) are both crucial players in this process. Topo IV removes DNA entanglements following the replication of the chromosome, whereas MukB, a member of the structural maintenance of chromosomes protein family, serves as a bacterial condensin. We demonstrate here a direct physical interaction between the dimerization domain of MukB and the C-terminal domain of the ParC subunit of Topo IV. In addition, we find that MukB alters the activity of Topo IV in vitro. Finally, we isolate a MukB mutant, D692A, that is deficient in its interaction with ParC and show that this mutant fails to rescue the temperature-sensitive growth phenotype of a mukB - strain. These results show that MukB and Topo IV are linked physically and functionally and indicate that the activities of these proteins are not limited to chromosome segregation but likely also play a key role in the control of higher-order bacterial chromosome structure.

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Section: Discussionsupporting

confidence: 77%

Escherichia coli condensin MukB stimulates topoisomerase IV activity by a direct physical interaction

Stewart

Berger

et al. 2010

Proc. Natl. Acad. Sci. U.S.A.

139

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“…In agreement, in vitro studies have shown that the core SMC heterodimer alone has DNA binding properties (23,41). Furthermore, short interfering RNAi depletion of human CAP-D2 from HeLa cells does not alter the levels of human CAP-E/SMC2 on mitotic chromosomes (48). In contrast, studies in budding yeast revealed that only the entire condensin complex is able to associate with DNA (25).…”

Section: Discussionmentioning

confidence: 99%

The Condensin I Subunit Barren/CAP-H Is Essential for the Structural Integrity of Centromeric Heterochromatin during Mitosis

Oliveira

Coelho

Sunkel

2005

Molecular and Cellular Biology

100

109

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During cell division, chromatin undergoes structural changes essential to ensure faithful segregation of the genome. Condensins, abundant components of mitotic chromosomes, are known to form two different complexes, condensins I and II. To further examine the role of condensin I in chromosome structure and in particular in centromere organization, we depleted from S2 cells the Drosophila CAP-H homologue Barren, a subunit exclusively associated with condensin I. In the absence of Barren/CAP-H the condensin core subunits DmSMC4/2 still associate with chromatin, while the other condensin I non-structural maintenance of chromosomes family proteins do not. Immunofluorescence and in vivo analysis of Barren/CAP-H-depleted cells showed that mitotic chromosomes are able to condense but fail to resolve sister chromatids. Additionally, Barren/CAP-H-depleted cells show chromosome congression defects that do not appear to be due to abnormal kinetochore-microtubule interaction. Instead, the centromeric and pericentromeric heterochromatin of Barren/CAP-H-depleted chromosomes shows structural problems. After bipolar attachment, the centromeric heterochromatin organized in the absence of Barren/CAP-H cannot withstand the forces exerted by the mitotic spindle and undergoes irreversible distortion. Taken together, our data suggest that the condensin I complex is required not only to promote sister chromatid resolution but also to maintain the structural integrity of centromeric heterochromatin during mitosis.

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“…It remains to be established, however, exactly how the two condensin complexes participate in the shaping and structural maintenance of metaphase chromatids (Gassmann et al 2004;Hirano 2005). The extent of defects observed in condensin-deficient cells varies among different conditions and different organisms, thereby leaving room for divergent interpretations (Hagstrom et al 2002;Coelho et al 2003;Hudson et al 2003;Chan et al 2004;Hirota et al 2004;Watrin and Legagneux 2005). Critical assignment of the role of individual subunits in vivo, along with a better understanding of their functions in vitro, will be essential in the future.…”

Section: Condensins and Chromosome Architecturementioning

confidence: 99%

Dynamic molecular linkers of the genome: the first decade of SMC proteins

Losada¹,

Hirano²

2005

Genes Dev.

330

311

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Structural maintenance of chromosomes (SMC) proteins are chromosomal ATPases, highly conserved from bacteria to humans, that play fundamental roles in many aspects of higher-order chromosome organization and dynamics. In eukaryotes, SMC1 and SMC3 act as the core of the cohesin complexes that mediate sister chromatid cohesion, whereas SMC2 and SMC4 function as the core of the condensin complexes that are essential for chromosome assembly and segregation. Another complex containing SMC5 and SMC6 is implicated in DNA repair and checkpoint responses. The SMC complexes form unique ring-or V-shaped structures with long coiled-coil arms, and function as ATP-modulated, dynamic molecular linkers of the genome. Recent studies shed new light on the mechanistic action of these SMC machines and also expanded the repertoire of their diverse cellular functions. Dissecting this class of chromosomal ATPases is likely to be central to our understanding of the structural basis of genome organization, stability, and evolution.The chromosome is at the heart of all genetic processes. Its precise duplication and segregation are arguably the most important goal of the mitotic cell cycle, and programmed expression of its content, either genetic or epigenetic, is central to the development of an organism. While the astonishing advancement of genome biology in recent years has provided an advanced starting point for virtually all areas in biology, it does not solve an old problem in chromosome biology: How is the genomic DNA folded, organized, and segregated in the tiny space of a cell? The discovery of structural maintenance of chromosomes (SMC) proteins, almost a decade ago, provided a decisive clue to solve this longstanding question, and led to the identification of cohesin and condensins, two representative classes of SMC-containing complexes in eukaryotes. The proposed actions of cohesin and condensins offer a plausible, if not complete, explanation for the sudden appearance of thread-like "substances" (the chromosomes) and their longitudinal splitting during mitosis, first described by Walther Flemming (1882). Remarkably, SMC proteins are conserved among the three phyla of life, indicating that the basic strategy of chromosome organization may be evolutionarily conserved from bacteria to humans. An emerging theme is that SMC proteins are dynamic molecular linkers of the genome that actively fold, tether, and manipulate DNA strands. Their diverse functions range far beyond chromosome segregation, and involve nearly all aspects of chromosome behavior including chromosome-wide or long-range gene regulation and DNA repair. In this review article, we summarize our current understanding of SMC proteins with a major focus on studies published during the past three years. We start by describing the architecture and mechanistic actions of SMC protein complexes, and then discuss how the concerted actions of cohesin and condensin support the faithful segregation of chromosomes during mitosis and meiosis. Finally, emerging studies of a third S...

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Contribution of hCAP-D2, a Non-SMC Subunit of Condensin I, to Chromosome and Chromosomal Protein Dynamics during Mitosis

Cited by 39 publications

References 65 publications

Escherichia coli condensin MukB stimulates topoisomerase IV activity by a direct physical interaction

Escherichia coli condensin MukB stimulates topoisomerase IV activity by a direct physical interaction

The Condensin I Subunit Barren/CAP-H Is Essential for the Structural Integrity of Centromeric Heterochromatin during Mitosis

Dynamic molecular linkers of the genome: the first decade of SMC proteins

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