ArticleNucleic acids research2019
The MLL1 trimeric catalytic complex is a dynamic conformational ensemble stabilized by multiple weak interactions.
Article in Nucleic acids research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 10 citations in OpenAlex.
- A Site-Specific Self-Association of a Protein Hub Drives Its Phase Separation.ACS chemical biology · 2026Article
- Neuron-specific WDR5 epigenetically upregulates ARID5B to impair GABAergic synaptic transmission and promotes epileptogenesis.Theranostics · 2026Article
- Interaction modules that impart specificity to disordered protein.Trends in biochemical sciences · 2023Review
- Bistable Photoswitch Allows in Vivo Control of Hematopoiesis.ACS central science · 2022Article
- Huntingtin structure is orchestrated by HAP40 and shows a polyglutamine expansion-specific interaction with exon 1.Communications biology · 2021Article
- Kinetics of the multitasking high-affinity Win binding site of WDR5 in restricted and unrestricted conditions.The Biochemical journal · 2021Article
- Mechanism for DPY30 and ASH2L intrinsically disordered regions to modulate the MLL/SET1 activity on chromatin.Nature communications · 2021Article
- Mixed-lineage leukaemia 1 contributes to endometrial stromal cells progesterone responsiveness during decidualization.Journal of cellular and molecular medicine · 2021Article
Corrections and comments
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Authors and funding
16 authors at 5 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Histone H3K4 methylation is an epigenetic mark associated with actively transcribed genes. This modification is catalyzed by the mixed lineage leukaemia (MLL) family of histone methyltransferases including MLL1, MLL2, MLL3, MLL4, SET1A and SET1B. The catalytic activity of this family is dependent on interactions with additional conserved proteins, but the structural basis for subunit assembly and the mechanism of regulation is not well understood. We used a hybrid methods approach to study the assembly and biochemical function of the minimally active MLL1 complex (MLL1, WDR5 and RbBP5). A combination of small angle X-ray scattering, cross-linking mass spectrometry, nuclear magnetic resonance spectroscopy and computational modeling were used to generate a dynamic ensemble model in which subunits are assembled via multiple weak interaction sites. We identified a new interaction site between the MLL1 SET domain and the WD40 β-propeller domain of RbBP5, and demonstrate the susceptibility of the catalytic function of the complex to disruption of individual interaction sites.
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