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  1. AU="Dang, Hung Q"
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  1. Article ; Online: Live-cell single-molecule tracking highlights requirements for stable Smc5/6 chromatin association in vivo.

    Etheridge, Thomas J / Villahermosa, Desiree / Campillo-Funollet, Eduard / Herbert, Alex David / Irmisch, Anja / Watson, Adam T / Dang, Hung Q / Osborne, Mark A / Oliver, Antony W / Carr, Antony M / Murray, Johanne M

    eLife

    2021  Volume 10

    Abstract: The essential Smc5/6 complex is required in response to replication stress and is best known for ensuring the fidelity of homologous recombination. Using single-molecule tracking in live fission yeast to investigate Smc5/6 chromatin association, we show ... ...

    Abstract The essential Smc5/6 complex is required in response to replication stress and is best known for ensuring the fidelity of homologous recombination. Using single-molecule tracking in live fission yeast to investigate Smc5/6 chromatin association, we show that Smc5/6 is chromatin associated in unchallenged cells and this depends on the non-SMC protein Nse6. We define a minimum of two Nse6-dependent sub-pathways, one of which requires the BRCT-domain protein Brc1. Using defined mutants in genes encoding the core Smc5/6 complex subunits, we show that the Nse3 double-stranded DNA binding activity and the arginine fingers of the two Smc5/6 ATPase binding sites are critical for chromatin association. Interestingly, disrupting the single-stranded DNA (ssDNA) binding activity at the hinge region does not prevent chromatin association but leads to elevated levels of gross chromosomal rearrangements during replication restart. This is consistent with a downstream function for ssDNA binding in regulating homologous recombination.
    MeSH term(s) Cell Cycle Proteins/metabolism ; Chromatin/metabolism ; Schizosaccharomyces/metabolism ; Schizosaccharomyces pombe Proteins/metabolism ; Single Molecule Imaging
    Chemical Substances Cell Cycle Proteins ; Chromatin ; Schizosaccharomyces pombe Proteins ; Smc5 protein, S pombe ; smc6 protein, S pombe
    Language English
    Publishing date 2021-04-16
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2687154-3
    ISSN 2050-084X ; 2050-084X
    ISSN (online) 2050-084X
    ISSN 2050-084X
    DOI 10.7554/eLife.68579
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Disruption of a ∼23-24 nucleotide small RNA pathway elevates DNA damage responses in

    Lee, Suzanne R / Pollard, Daniel A / Galati, Domenico F / Kelly, Megan L / Miller, Brian / Mong, Christina / Morris, Megan N / Roberts-Nygren, Kerry / Kapler, Geoffrey M / Zinkgraf, Matthew / Dang, Hung Q / Branham, Erica / Sasser, Jason / Tessier, Erin / Yoshiyama, Courtney / Matsumoto, Maya / Turman, Gaea

    Molecular biology of the cell

    2021  Volume 32, Issue 15, Page(s) 1335–1346

    Abstract: Endogenous RNA interference (RNAi) pathways regulate a wide range of cellular processes in diverse eukaryotes, yet in the ciliated eukaryote, ...

    Abstract Endogenous RNA interference (RNAi) pathways regulate a wide range of cellular processes in diverse eukaryotes, yet in the ciliated eukaryote,
    MeSH term(s) DNA/metabolism ; DNA Breaks, Double-Stranded ; DNA Repair ; Evolution, Molecular ; Gene Expression Profiling ; Gene Expression Regulation ; Protozoan Proteins ; RNA, Small Interfering/metabolism ; Rad51 Recombinase/genetics ; Recombinational DNA Repair ; Sequence Analysis, RNA ; Tetrahymena thermophila/genetics ; Tetrahymena thermophila/metabolism
    Chemical Substances Protozoan Proteins ; RNA, Small Interfering ; DNA (9007-49-2) ; Rad51 Recombinase (EC 2.7.7.-)
    Language English
    Publishing date 2021-05-19
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 1098979-1
    ISSN 1939-4586 ; 1059-1524
    ISSN (online) 1939-4586
    ISSN 1059-1524
    DOI 10.1091/mbc.E20-10-0631
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 2853: Show issues Location:
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    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
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    Zs.MO 410: Show issues

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  3. Article ; Online: Specialized interfaces of Smc5/6 control hinge stability and DNA association.

    Alt, Aaron / Dang, Hung Q / Wells, Owen S / Polo, Luis M / Smith, Matt A / McGregor, Grant A / Welte, Thomas / Lehmann, Alan R / Pearl, Laurence H / Murray, Johanne M / Oliver, Antony W

    Nature communications

    2017  Volume 8, Page(s) 14011

    Abstract: The Structural Maintenance of Chromosomes (SMC) complexes: cohesin, condensin and Smc5/6 are involved in the organization of higher-order chromosome structure-which is essential for accurate chromosome duplication and segregation. Each complex is ... ...

    Abstract The Structural Maintenance of Chromosomes (SMC) complexes: cohesin, condensin and Smc5/6 are involved in the organization of higher-order chromosome structure-which is essential for accurate chromosome duplication and segregation. Each complex is scaffolded by a specific SMC protein dimer (heterodimer in eukaryotes) held together via their hinge domains. Here we show that the Smc5/6-hinge, like those of cohesin and condensin, also forms a toroidal structure but with distinctive subunit interfaces absent from the other SMC complexes; an unusual 'molecular latch' and a functional 'hub'. Defined mutations in these interfaces cause severe phenotypic effects with sensitivity to DNA-damaging agents in fission yeast and reduced viability in human cells. We show that the Smc5/6-hinge complex binds preferentially to ssDNA and that this interaction is affected by both 'latch' and 'hub' mutations, suggesting a key role for these unique features in controlling DNA association by the Smc5/6 complex.
    MeSH term(s) Adenosine Triphosphatases/chemistry ; Binding Sites ; Cell Cycle Proteins/chemistry ; Cell Cycle Proteins/genetics ; Cell Cycle Proteins/metabolism ; Cell Line, Tumor ; Cell Survival/physiology ; Chromosomal Proteins, Non-Histone/chemistry ; Chromosomal Proteins, Non-Histone/genetics ; Chromosomal Proteins, Non-Histone/metabolism ; Crystallography, X-Ray ; DNA Damage ; DNA Repair/physiology ; DNA, Single-Stranded/metabolism ; DNA-Binding Proteins/chemistry ; Humans ; Models, Molecular ; Multiprotein Complexes/chemistry ; Mutagenesis, Site-Directed ; Mutation ; Phenotype ; Protein Binding ; Protein Domains/physiology ; Protein Multimerization/physiology ; Recombinant Proteins/chemistry ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; Schizosaccharomyces/physiology ; Schizosaccharomyces pombe Proteins/chemistry ; Schizosaccharomyces pombe Proteins/genetics ; Schizosaccharomyces pombe Proteins/metabolism ; Cohesins
    Chemical Substances Cell Cycle Proteins ; Chromosomal Proteins, Non-Histone ; DNA, Single-Stranded ; DNA-Binding Proteins ; Multiprotein Complexes ; Recombinant Proteins ; SMC5 protein, human ; SMC6 protein, human ; Schizosaccharomyces pombe Proteins ; Smc5 protein, S pombe ; condensin complexes ; smc6 protein, S pombe ; Adenosine Triphosphatases (EC 3.6.1.-)
    Language English
    Publishing date 2017-01-30
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/ncomms14011
    Database MEDical Literature Analysis and Retrieval System OnLINE

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