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MeCP2 Interacts with the Super Elongation Complex to Regulate Transcription

ABSTRACT: This SuperSeries is composed of the SubSeries listed below.

ORGANISM(S): Mus musculus

PROVIDER: GSE275333 | GEO | 2025/11/03

REPOSITORIES: GEO

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MeCP2 Interacts with the Super Elongation Complex to Regulate Transcription (RNA-Seq)

Project description:Loss-of-function mutations in methyl-CpG binding protein 2 (MECP2) cause the neurodevelopmental disorder, Rett syndrome (RTT). The molecular mechanisms underlying MeCP2 function remain poorly understood. Here, using a MECP2 gain-of-function Drosophila model, we screened for genetic modifiers of MECP2-induced toxicity. Our approach identified several subunits of the Drosophila super elongation complex (SEC), a P-TEFb containing elongation factor that releases promoter-proximally paused RNA polymerase II (RNA pol II), as genetic interactors of MECP2. MeCP2 directly interacts with AFF4, the scaffold of the SEC, and facilitates its binding on a subset of genes that regulate neuronal development and synaptic function in the mouse cortex. Furthermore, genes with reduced AFF4 binding showed reduced RNA pol II binding in their genebody and decreased RNA expression in Mecp2 null mice. Taken together, we propose that MeCP2 interacts with the SEC to facilitate the release of RNA pol II and thereby support gene expression.

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MeCP2 Interacts with the Super Elongation Complex to Regulate Transcription (ChIP-Seq)

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MeCP2 Interacts with the Super Elongation Complex to Regulate Transcription

Project description:MeCP2 Interacts with the Super Elongation Complex to Regulate Transcription

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MeCP2 Interacts with the Super Elongation Complex to Regulate Transcription (ChIP-Seq)

Project description:MeCP2 Interacts with the Super Elongation Complex to Regulate Transcription (ChIP-Seq)

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Allosteric transcription stimulation by super elongation complex

Project description:The super elongation complex (SEC) contains the positive transcription elongation factor b (P-TEFb) and a subcomplex, ELL2-EAF1, which stimulates transcription elongation by RNA polymerase II (Pol II). Here we report the cryo-EM structure of ELL2-EAF1 bound to a Pol II elongation complex at 2.8 Å resolution. The ELL2-EAF1 dimerization module directly binds the Pol II lobe, explaining how SEC delivers P-TEFb to Pol II. The same site on the lobe also binds the initiation factor TFIIF, consistent with SEC binding only after the transition from transcription initiation to elongation. Structure-guided functional analysis shows that elongation stimulation requires the dimerization module and an ELL2 protein linker that tethers this module to the Pol II protrusion. Our results show that SEC stimulates elongation allosterically and indicate that this stimulation involves stabilization of a further closed conformation of the Pol II active center cleft.

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