Human Rad50/Mre11 is a flexible complex that can tether DNA ends (Q28210390)

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J van Noort

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D C van Gent

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R Kanaar

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C Wyman

Structure of the Rad50 x Mre11 DNA repair complex from Saccharomyces cerevisiae by electron microscopy

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language of work or name

English

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publication date

November 2001

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published in

Molecular Cell

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volume

8

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issue

5

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page(s)

1129-35

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cites work

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Role of the human RAD51 protein in homologous recombination and double-stranded-break repair

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Scanning force microscopy of nucleic acids and nucleoprotein assemblies

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The hMre11/hRad50 protein complex and Nijmegen breakage syndrome: linkage of double-strand break repair to the cellular DNA damage response

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Promotion of Dnl4-catalyzed DNA end-joining by the Rad50/Mre11/Xrs2 and Hdf1/Hdf2 complexes

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The SbcCD nuclease of Escherichia coli is a structural maintenance of chromosomes (SMC) family protein that cleaves hairpin DNA

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Recombinational repair of chromosomal DNA double-strand breaks generated by a restriction endonuclease

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DNA-binding and strand-annealing activities of human Mre11: implications for its roles in DNA double-strand break repair pathways

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Human Rad50 is physically associated with human Mre11: identification of a conserved multiprotein complex implicated in recombinational DNA repair

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A novel SMC protein complex in Schizosaccharomyces pombe contains the Rad18 DNA repair protein

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Bimodal activation of SMC ATPase by intra- and inter-molecular interactions

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Closing the ring: links between SMC proteins and chromosome partitioning, condensation, and supercoiling

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Structural biology of Rad50 ATPase: ATP-driven conformational control in DNA double-strand break repair and the ABC-ATPase superfamily

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Structural biochemistry and interaction architecture of the DNA double-strand break repair Mre11 nuclease and Rad50-ATPase

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Molecular mechanisms of DNA double strand break repair

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DNA double strand break repair in mammalian cells

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Tying up loose ends: nonhomologous end-joining in Saccharomyces cerevisiae

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Crystal structure of the SMC head domain: an ABC ATPase with 900 residues antiparallel coiled-coil inserted

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Disruption of mRad50 causes embryonic stem cell lethality, abnormal embryonic development, and sensitivity to ionizing radiation

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The symmetrical structure of structural maintenance of chromosomes (SMC) and MukB proteins: long, antiparallel coiled coils, folded at a flexible hinge

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DNA repair: spot(light)s on chromatin.

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Functions of the yeast meiotic recombination genes, MRE11 and MRE2.

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X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil

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The 3' to 5' exonuclease activity of Mre 11 facilitates repair of DNA double-strand breaks

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A mechanistic basis for Mre11-directed DNA joining at microhomologies

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7 January 2021

The architecture of the human Rad54-DNA complex provides evidence for protein translocation along DNA

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Polymer chain statistics and conformational analysis of DNA molecules with bends or sections of different flexibility

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The SMC proteins and the coming of age of the chromosome scaffold hypothesis.

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7 January 2021

Structural and functional similarities between the SbcCD proteins of Escherichia coli and the RAD50 and MRE11 (RAD32) recombination and repair proteins of yeast.

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The DNA double-strand break repair gene hMRE11 is mutated in individuals with an ataxia-telangiectasia-like disorder

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Structural maintenance of chromosomes (SMC) proteins: conserved molecular properties for multiple biological functions

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Recombination factors of Saccharomyces cerevisiae

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Nuclease activities in a complex of human recombination and DNA repair factors Rad50, Mre11, and p95

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Complex formation and functional versatility of Mre11 of budding yeast in recombination

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Unusual oligomerization required for activity of NtrC, a bacterial enhancer-binding protein

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Conditional gene targeted deletion by Cre recombinase demonstrates the requirement for the double-strand break repair Mre11 protein in murine embryonic stem cells

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Targeted disruption of the Nijmegen breakage syndrome gene NBS1 leads to early embryonic lethality in mice.

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