Literature DB >> 16168369

A nanomachine for making ends meet: MRN is a flexing scaffold for the repair of DNA double-strand breaks.

R Scott Williams1, John A Tainer.   

Abstract

In a recent study (Moreno-Herrero et al., 2005), atomic force microscopy (AFM) imaging of the human Mre11/Rad50/Nbs1 (MRN) complex engaging substrate DNA revealed large-scale, DNA binding-induced propagation of conformational change to the distal ends of the Rad50 coiled coils and erection of a 1000 A scaffold to productively bridge DNA ends.

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Year:  2005        PMID： 16168369     DOI： 10.1016/j.molcel.2005.07.006

Source DB:  PubMed          Journal:  Mol Cell        ISSN： 1097-2765            Impact factor:   17.970


  15 in total

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Review 3.  Recognition and repair of chemically heterogeneous structures at DNA ends.

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Review 4.  Ataxia-telangiectasia and related diseases.

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5.  Cell cycle-dependent role of MRN at dysfunctional telomeres: ATM signaling-dependent induction of nonhomologous end joining (NHEJ) in G1 and resection-mediated inhibition of NHEJ in G2.

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Journal:  Mol Cell Biol       Date:  2009-08-10       Impact factor: 4.272

Review 6.  Envisioning the dynamics and flexibility of Mre11-Rad50-Nbs1 complex to decipher its roles in DNA replication and repair.

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Journal:  Prog Biophys Mol Biol       Date:  2015-01-07       Impact factor: 3.667

7.  Interdependence of the rad50 hook and globular domain functions.

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Journal:  Mol Cell       Date:  2015-01-15       Impact factor: 17.970

8.  Mre11 nuclease activity has essential roles in DNA repair and genomic stability distinct from ATM activation.

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9.  Coprinus cinereus rad50 mutants reveal an essential structural role for Rad50 in axial element and synaptonemal complex formation, homolog pairing and meiotic recombination.

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10.  Inhibition of transcription at radiation-induced nuclear foci of phosphorylated histone H2AX in mammalian cells.

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