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  1. Article ; Online: Resolving complex chromosome structures during meiosis: versatile deployment of Smc5/6.

    Verver, Dideke E / Hwang, Grace H / Jordan, Philip W / Hamer, Geert

    Chromosoma

    2016  Volume 125, Issue 1, Page(s) 15–27

    Abstract: The Smc5/6 complex, along with cohesin and condensin, is a member of the structural maintenance of chromosome (SMC) family, large ring-like protein complexes that are essential for chromatin structure and function. Thanks to numerous studies of the ... ...

    Abstract The Smc5/6 complex, along with cohesin and condensin, is a member of the structural maintenance of chromosome (SMC) family, large ring-like protein complexes that are essential for chromatin structure and function. Thanks to numerous studies of the mitotic cell cycle, Smc5/6 has been implicated to have roles in homologous recombination, restart of stalled replication forks, maintenance of ribosomal DNA (rDNA) and heterochromatin, telomerase-independent telomere elongation, and regulation of chromosome topology. The nature of these functions implies that the Smc5/6 complex also contributes to the profound chromatin changes, including meiotic recombination, that characterize meiosis. Only recently, studies in diverse model organisms have focused on the potential meiotic roles of the Smc5/6 complex. Indeed, Smc5/6 appears to be essential for meiotic recombination. However, due to both the complexity of the process of meiosis and the versatility of the Smc5/6 complex, many additional meiotic functions have been described. In this review, we provide a clear overview of the multiple functions found so far for the Smc5/6 complex in meiosis. Additionally, we compare these meiotic functions with the known mitotic functions in an attempt to find a common denominator and thereby create clarity in the field of Smc5/6 research.
    MeSH term(s) Animals ; Cell Cycle Proteins/physiology ; Chromatin/metabolism ; Chromosome Segregation ; DNA/metabolism ; DNA Repair ; DNA Replication ; Homologous Recombination ; Humans ; Meiosis/genetics ; Saccharomyces cerevisiae Proteins/physiology ; Telomere/metabolism ; Yeasts/metabolism
    Chemical Substances Cell Cycle Proteins ; Chromatin ; SMC5 protein, S cerevisiae ; SMC5 protein, human ; SMC6 protein, S cerevisiae ; SMC6 protein, human ; Saccharomyces cerevisiae Proteins ; DNA (9007-49-2)
    Language English
    Publishing date 2016-03
    Publishing country Austria
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 203083-4
    ISSN 1432-0886 ; 0009-5915
    ISSN (online) 1432-0886
    ISSN 0009-5915
    DOI 10.1007/s00412-015-0518-9
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

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  2. Article ; Online: The SMC5/6 complex is involved in crucial processes during human spermatogenesis.

    Verver, Dideke E / Langedijk, Nathalia S M / Jordan, Philip W / Repping, Sjoerd / Hamer, Geert

    Biology of reproduction

    2014  Volume 91, Issue 1, Page(s) 22

    Abstract: Genome integrity is crucial for safe reproduction. Therefore, chromatin structure and dynamics should be tightly regulated during germ cell development. Chromatin structure and function are in large part determined by the structural maintenance of ... ...

    Abstract Genome integrity is crucial for safe reproduction. Therefore, chromatin structure and dynamics should be tightly regulated during germ cell development. Chromatin structure and function are in large part determined by the structural maintenance of chromosomes (SMC) protein complexes, of which SMC5/6 recently has been shown to be involved in both spermatogonial differentiation and meiosis during mouse spermatogenesis. We therefore investigated the role of this complex in human spermatogenesis. We found SMC6 to be expressed in the human testis and present in a subset of type Adark and type Apale spermatogonia, all spermatocytes, and round spermatids. During human meiosis, SMC5/6 is located at the synaptonemal complex (SC), the XY body, and at the centromeres during meiotic metaphases. However, in contrast to mouse spermatogenesis, SMC6 is not located at pericentromeric heterochromatin in human spermatogenic cells, indicating subtle but perhaps important differences in not only SMC5/6 function but maybe also in maintenance of genomic integrity at the repetitive pericentromeric regions. Nonetheless, our data clearly indicate that the SMC5/6 complex, as shown in mice, is involved in numerous crucial processes during human spermatogenesis, such as in spermatogonial development, on the SC between synapsed chromosomes, and in DNA double-strand break repair on unsynapsed chromosomes during pachynema.
    MeSH term(s) Cell Cycle Proteins/metabolism ; Chromosomal Proteins, Non-Histone ; Humans ; Male ; Meiosis/physiology ; Spermatids/metabolism ; Spermatocytes/metabolism ; Spermatogenesis/physiology ; Spermatogonia/metabolism ; Testis/metabolism
    Chemical Substances Cell Cycle Proteins ; Chromosomal Proteins, Non-Histone ; SMC5 protein, human ; SMC6 protein, human
    Language English
    Publishing date 2014-05-22
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1118-6
    ISSN 1529-7268 ; 0006-3363
    ISSN (online) 1529-7268
    ISSN 0006-3363
    DOI 10.1095/biolreprod.114.118596
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 551: Show issues Location:
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  3. Article ; Online: Non-SMC Element 2 (NSMCE2) of the SMC5/6 Complex Helps to Resolve Topological Stress

    Dideke E. Verver / Yi Zheng / Dave Speijer / Ron Hoebe / Henk L. Dekker / Sjoerd Repping / Jan Stap / Geert Hamer

    International Journal of Molecular Sciences, Vol 17, Iss 11, p

    2016  Volume 1782

    Abstract: The structural maintenance of chromosomes (SMC) protein complexes shape and regulate the structure and dynamics of chromatin, thereby controlling many chromosome-based processes such as cell cycle progression, differentiation, gene transcription and DNA ... ...

    Abstract The structural maintenance of chromosomes (SMC) protein complexes shape and regulate the structure and dynamics of chromatin, thereby controlling many chromosome-based processes such as cell cycle progression, differentiation, gene transcription and DNA repair. The SMC5/6 complex is previously described to promote DNA double-strand breaks (DSBs) repair by sister chromatid recombination, and found to be essential for resolving recombination intermediates during meiotic recombination. Moreover, in budding yeast, SMC5/6 provides structural organization and topological stress relief during replication in mitotically dividing cells. Despite the essential nature of the SMC5/6 complex, the versatile mechanisms by which SMC5/6 functions and its molecular regulation in mammalian cells remain poorly understood. By using a human osteosarcoma cell line (U2OS), we show that after the CRISPR-Cas9-mediated removal of the SMC5/6 subunit NSMCE2, treatment with the topoisomerase II inhibitor etoposide triggered an increased sensitivity in cells lacking NSMCE2. In contrast, NSMCE2 appeared not essential for a proper DNA damage response or cell survival after DSB induction by ionizing irradiation (IR). Interestingly, by way of immunoprecipitations (IPs) and mass spectrometry, we found that the SMC5/6 complex physically interacts with the DNA topoisomerase II α (TOP2A). We therefore propose that the SMC5/6 complex functions in resolving TOP2A-mediated DSB-repair intermediates generated during replication.
    Keywords Structural Maintenance of Chromosomes 5/6 complex (SMC5/6) ; Non-SMC Element 2 (NSMCE2) ; Topoisomerase II α (TOP2A) ; DNA double-strand breaks (DSBs) ; Ionizing Radiation (IR) ; CRISPR-Cas9 ; Biology (General) ; QH301-705.5 ; Chemistry ; QD1-999
    Subject code 612
    Language English
    Publishing date 2016-10-01T00:00:00Z
    Publisher MDPI AG
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  4. Article ; Online: Non-SMC Element 2 (NSMCE2) of the SMC5/6 Complex Helps to Resolve Topological Stress.

    Verver, Dideke E / Zheng, Yi / Speijer, Dave / Hoebe, Ron / Dekker, Henk L / Repping, Sjoerd / Stap, Jan / Hamer, Geert

    International journal of molecular sciences

    2016  Volume 17, Issue 11

    Abstract: The structural maintenance of chromosomes (SMC) protein complexes shape and regulate the structure and dynamics of chromatin, thereby controlling many chromosome-based processes such as cell cycle progression, differentiation, gene transcription and DNA ... ...

    Abstract The structural maintenance of chromosomes (SMC) protein complexes shape and regulate the structure and dynamics of chromatin, thereby controlling many chromosome-based processes such as cell cycle progression, differentiation, gene transcription and DNA repair. The SMC5/6 complex is previously described to promote DNA double-strand breaks (DSBs) repair by sister chromatid recombination, and found to be essential for resolving recombination intermediates during meiotic recombination. Moreover, in budding yeast, SMC5/6 provides structural organization and topological stress relief during replication in mitotically dividing cells. Despite the essential nature of the SMC5/6 complex, the versatile mechanisms by which SMC5/6 functions and its molecular regulation in mammalian cells remain poorly understood. By using a human osteosarcoma cell line (U2OS), we show that after the CRISPR-Cas9-mediated removal of the SMC5/6 subunit NSMCE2, treatment with the topoisomerase II inhibitor etoposide triggered an increased sensitivity in cells lacking NSMCE2. In contrast, NSMCE2 appeared not essential for a proper DNA damage response or cell survival after DSB induction by ionizing irradiation (IR). Interestingly, by way of immunoprecipitations (IPs) and mass spectrometry, we found that the SMC5/6 complex physically interacts with the DNA topoisomerase II α (TOP2A). We therefore propose that the SMC5/6 complex functions in resolving TOP2A-mediated DSB-repair intermediates generated during replication.
    MeSH term(s) Antigens, Neoplasm/metabolism ; CRISPR-Cas Systems ; Cell Cycle Proteins/genetics ; Cell Cycle Proteins/metabolism ; Cell Line, Tumor ; Cell Survival/radiation effects ; DNA Breaks, Double-Stranded/drug effects ; DNA Breaks, Double-Stranded/radiation effects ; DNA Repair ; DNA Topoisomerases, Type II/metabolism ; DNA-Binding Proteins/metabolism ; Etoposide/adverse effects ; Humans ; Ligases/genetics ; Ligases/metabolism ; Poly-ADP-Ribose Binding Proteins ; Protein Interaction Maps ; Topoisomerase II Inhibitors/adverse effects
    Chemical Substances Antigens, Neoplasm ; Cell Cycle Proteins ; DNA-Binding Proteins ; Poly-ADP-Ribose Binding Proteins ; SMC5 protein, human ; SMC6 protein, human ; Topoisomerase II Inhibitors ; Etoposide (6PLQ3CP4P3) ; DNA Topoisomerases, Type II (EC 5.99.1.3) ; TOP2A protein, human (EC 5.99.1.3) ; Ligases (EC 6.-) ; NSMCE2 protein, human (EC 6.3.2.-)
    Language English
    Publishing date 2016-10-26
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2019364-6
    ISSN 1422-0067 ; 1422-0067 ; 1661-6596
    ISSN (online) 1422-0067
    ISSN 1422-0067 ; 1661-6596
    DOI 10.3390/ijms17111782
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Disruption of a ciliary B9 protein complex causes Meckel syndrome.

    Dowdle, William E / Robinson, Jon F / Kneist, Andreas / Sirerol-Piquer, M Salomé / Frints, Suzanna G M / Corbit, Kevin C / Zaghloul, Norann A / Zaghloul, Norran A / van Lijnschoten, Gesina / Mulders, Leon / Verver, Dideke E / Zerres, Klaus / Reed, Randall R / Attié-Bitach, Tania / Johnson, Colin A / García-Verdugo, José Manuel / Katsanis, Nicholas / Bergmann, Carsten / Reiter, Jeremy F

    American journal of human genetics

    2011  Volume 89, Issue 1, Page(s) 94–110

    Abstract: Nearly every ciliated organism possesses three B9 domain-containing proteins: MKS1, B9D1, and B9D2. Mutations in human MKS1 cause Meckel syndrome (MKS), a severe ciliopathy characterized by occipital encephalocele, liver ductal plate malformations, ... ...

    Abstract Nearly every ciliated organism possesses three B9 domain-containing proteins: MKS1, B9D1, and B9D2. Mutations in human MKS1 cause Meckel syndrome (MKS), a severe ciliopathy characterized by occipital encephalocele, liver ductal plate malformations, polydactyly, and kidney cysts. Mouse mutations in either Mks1 or B9d2 compromise ciliogenesis and result in phenotypes similar to those of MKS. Given the importance of these two B9 proteins to ciliogenesis, we examined the role of the third B9 protein, B9d1. Mice lacking B9d1 displayed polydactyly, kidney cysts, ductal plate malformations, and abnormal patterning of the neural tube, concomitant with compromised ciliogenesis, ciliary protein localization, and Hedgehog (Hh) signal transduction. These data prompted us to screen MKS patients for mutations in B9D1 and B9D2. We identified a homozygous c.301A>C (p.Ser101Arg) B9D2 mutation that segregates with MKS, affects an evolutionarily conserved residue, and is absent from controls. Unlike wild-type B9D2 mRNA, the p.Ser101Arg mutation failed to rescue zebrafish phenotypes induced by the suppression of b9d2. With coimmunoprecipitation and mass spectrometric analyses, we found that Mks1, B9d1, and B9d2 interact physically, but that the p.Ser101Arg mutation abrogates the ability of B9d2 to interact with Mks1, further suggesting that the mutation compromises B9d2 function. Our data indicate that B9d1 is required for normal Hh signaling, ciliogenesis, and ciliary protein localization and that B9d1 and B9d2 are essential components of a B9 protein complex, disruption of which causes MKS.
    MeSH term(s) Amino Acid Sequence ; Animals ; Ciliary Motility Disorders/genetics ; DNA Mutational Analysis ; Encephalocele/genetics ; Genetic Linkage ; Homozygote ; Humans ; Mice ; Mice, Inbred C57BL ; Molecular Sequence Data ; Mutation ; NIH 3T3 Cells ; Neural Tube/abnormalities ; Phenotype ; Polycystic Kidney Diseases/genetics ; Polydactyly/genetics ; Protein Transport/genetics ; Proteins/genetics ; Proteins/metabolism ; RNA, Messenger/genetics ; RNA, Messenger/metabolism ; Retinitis Pigmentosa ; Signal Transduction ; Zebrafish/genetics
    Chemical Substances MKS1 protein, mouse ; Proteins ; RNA, Messenger
    Language English
    Publishing date 2011-07-07
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 219384-x
    ISSN 1537-6605 ; 0002-9297
    ISSN (online) 1537-6605
    ISSN 0002-9297
    DOI 10.1016/j.ajhg.2011.06.003
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 107: Show issues Location:
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