The ends in sight: Mre11-Rad50-Nbs1 complex structures come into focus

Jessica L Wojtaszek; R Scott Williams

doi:10.1016/j.molcel.2022.12.016

The ends in sight: Mre11-Rad50-Nbs1 complex structures come into focus

Mol Cell. 2023 Jan 19;83(2):160-162. doi: 10.1016/j.molcel.2022.12.016.

Authors

Jessica L Wojtaszek¹, R Scott Williams²

Affiliations

¹ Genome Integrity and Structural Biology Laboratory, National Institute of Environmental Health Sciences, US National Institutes of Health, Department of Health and Human Services, Durham, Research Triangle Park, NC 27709, USA.
² Genome Integrity and Structural Biology Laboratory, National Institute of Environmental Health Sciences, US National Institutes of Health, Department of Health and Human Services, Durham, Research Triangle Park, NC 27709, USA. Electronic address: [email protected].

PMID: 36669476
DOI: 10.1016/j.molcel.2022.12.016

Abstract

In this issue of Molecular Cell, Rotheneder et al.¹ elucidate the eukaroytic Mre11-Rad50-Nbs1 (MRN) complex quaternary architecture, which together with cryo-EM structures of bacterial Mre11-Rad50-DNA complexes,² resolves the basis for MRN assembly and its broad nuclease specificity regulating DNA double-strand break repair.

Published by Elsevier Inc.

MeSH terms

Acid Anhydride Hydrolases / genetics
Cell Cycle Proteins* / genetics
Cell Cycle Proteins* / metabolism
DNA / genetics
DNA Repair
DNA Repair Enzymes* / genetics
DNA Repair Enzymes* / metabolism
MRE11 Homologue Protein / genetics
Nuclear Proteins / genetics
Nuclear Proteins / metabolism

Substances

MRE11 Homologue Protein
Cell Cycle Proteins
DNA Repair Enzymes
Nuclear Proteins
DNA
Acid Anhydride Hydrolases