ArticleCell research2014
The histone-fold complex MHF is remodeled by FANCM to recognize branched DNA and protect genome stability.
Article in Cell research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 23 citations in OpenAlex.
- Machine learning reveals complex genetics of fungal resistance in sorghum grain mold.Heredity · 2025Article
- Identifying an AML Prognostic Model Using 10 Marker Genes from Single-Cell Transcriptome and Bulk Transcriptome Analysis.Biochemical genetics · 2024Article
- Biochemical and crystallization analysis of the CENP-SX-DNA complex.Acta crystallographica. Section F, Structural biology communications · 2022Article
- Structural analysis of the chicken FANCM-MHF complex and its stability.Acta crystallographica. Section F, Structural biology communications · 2021Article
- Article
- The FANCM-BLM-TOP3A-RMI complex suppresses alternative lengthening of telomeres (ALT).Nature communications · 2019Article
- Therapeutic Silencing of Centromere Protein X Ameliorates Hyperglycemia in Zebrafish and Mouse Models of Type 2 Diabetes Mellitus.Frontiers in genetics · 2019Article
- Bloom syndrome complex promotes FANCM recruitment to stalled replication forks and facilitates both repair and traverse of DNA interstrand crosslinks.Cell discovery · 2016Article
- FANCI Regulates Recruitment of the FA Core Complex at Sites of DNA Damage Independently of FANCD2.PLoS genetics · 2015Article
- Protein-Protein Interactions Mediated by Helical Tertiary Structure Motifs.Journal of the American Chemical Society · 2015Article
- Functions and regulation of the multitasking FANCM family of DNA motor proteins.Genes & development · 2015Review
- Selective modulation of the functions of a conserved DNA motor by a histone fold complex.Genes & development · 2015Article
- Replication fork reversal in eukaryotes: from dead end to dynamic response.Nature reviews. Molecular cell biology · 2015Review
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
Histone-fold proteins typically assemble in multiprotein complexes to bind duplex DNA. However, one histone-fold complex, MHF, associates with Fanconi anemia (FA) protein FANCM to form a branched DNA remodeling complex that senses and repairs stalled replication forks and activates FA DNA damage response network. How the FANCM-MHF complex recognizes branched DNA is unclear. Here, we solved the crystal structure of MHF and its complex with the MHF-interaction domain (referred to as MID) of FANCM, and performed structure-guided mutagenesis. We found that the MID-MHF complex consists of one histone H3-H4-like MHF heterotetramer wrapped by a single polypeptide of MID. We identified a zinc atom-liganding structure at the central interface between MID and MHF that is critical for stabilization of the complex. Notably, the DNA-binding surface of MHF was altered by MID in both electrostatic charges and allosteric conformation. This leads to a switch in the DNA-binding preference - from duplex DNA by MHF alone, to branched DNA by the MID-MHF complex. Mutations that disrupt either the composite DNA-binding surface or the protein-protein interface of the MID-MHF complex impaired activation of the FA network and genome stability. Our data provide the structural basis of how FANCM and MHF work together to recognize branched DNA, and suggest a novel mechanism by which histone-fold complexes can be remodeled by their partners to bind special DNA structures generated during DNA metabolism.
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