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

R Scott Williams; John A Tainer

doi:10.1016/j.molcel.2005.07.006

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

Mol Cell. 2005 Sep 16;19(6):724-6. doi: 10.1016/j.molcel.2005.07.006.

Authors

R Scott Williams¹, John A Tainer

Affiliation

¹ Department of Molecular Biology and The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, California 92037, USA.

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

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.

Publication types

Comment

MeSH terms

Acid Anhydride Hydrolases
Cell Cycle Proteins* / chemistry
Cell Cycle Proteins* / metabolism
DNA Damage
DNA Repair
DNA Repair Enzymes* / chemistry
DNA Repair Enzymes* / metabolism
DNA-Binding Proteins* / chemistry
DNA-Binding Proteins* / metabolism
Humans
MRE11 Homologue Protein
Models, Molecular
Nuclear Proteins* / chemistry
Nuclear Proteins* / metabolism
Nucleic Acid Conformation*

Substances

Cell Cycle Proteins
DNA-Binding Proteins
MRE11 protein, human
NBN protein, human
Nuclear Proteins
MRE11 Homologue Protein
Acid Anhydride Hydrolases
RAD50 protein, human
DNA Repair Enzymes