Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

The GNMT N-terminus Couples Folate Feedback to Methyl-donor Homeostasis.

bioRxiv : the preprint server for biology·2026

Same author

Recommendations and considerations for hydroxyl radical protein footprinting-mass spectrometry.

Nature methods·2026

Same author

Determinants of DNA-sequence-based Diagnostic Yield in the CSER Consortium.

medRxiv : the preprint server for health sciences·2026

Same author

Understanding the Role of Functional Noncoding Variation in Human Diseases with Lessons from Immunity.

Annual review of genomics and human genetics·2026

Same author

Integrating multi-omic QTLs and predictive models reveals regulatory architectures at immune related GWAS loci in CD4+ T cells.

medRxiv : the preprint server for health sciences·2026

Same author

Egr1 is a sex-dependent regulator of neuronal chromatin, structural plasticity, and behaviour.

Nature communications·2025

Same journal

Aromatic Cage-Directed Azide-Methyllysine Photochemistry for Profiling Nonhistone Interacting Partners of the MeCP2 Methyl-CpG-Binding Domain.

Biochemistry·2026

Same journal

Differential Hydroxypyruvate Processing by <i>E. coli</i> and <i>P. aeruginosa</i> DXP Synthases Reveals Preferential Xylulose 5-Phosphate Formation by the <i>P. aeruginosa</i> Enzyme.

Biochemistry·2026

Same journal

Structural and Functional Characterization of Heterologous Nitrogenase Complexes.

Biochemistry·2026

Same journal

Discovery of Bacterial Unspecific Peroxygenases.

Biochemistry·2026

Same journal

Lactate Biology: Subcellular Routing and Chemical Form Define Function.

Biochemistry·2026

Same journal

Nature's Anaerobic Toolkit: Glycyl Radical Enzymes and Their Expanding Functional and Mechanistic Diversity.

Biochemistry·2026

See all related articles

Search research articles

Related Experiment Video

Updated: Dec 25, 2025

An Electrochemiluminescence-Based Assay for MeCP2 Protein Variants

An Electrochemiluminescence-Based Assay for MeCP2 Protein Variants

Published on: May 22, 2020

MeCP2 Binding Cooperativity Inhibits DNA Modification-Specific Recognition.

Sergei Khrapunov¹, Yisong Tao¹, Huiyong Cheng¹

¹Department of Biochemistry, ‡Departments of Neurology and Neuroscience, and §Department of Genetics, Albert Einstein College of Medicine , 1300 Morris Park Avenue, Bronx, New York 10461, United States.

|July 16, 2016

Summary

This summary is machine-generated.

Methyl-CpG binding protein 2 (MeCP2) binding to DNA is influenced by ion concentration and type, affecting neuronal development. Polypeptide flexibility and binding cooperativity are key to MeCP2’s function.

More Related Videos

Repressing Gene Transcription by Redirecting Cellular Machinery with Chemical Epigenetic Modifiers

Repressing Gene Transcription by Redirecting Cellular Machinery with Chemical Epigenetic Modifiers

Published on: September 20, 2018

Immunostaining for DNA Modifications: Computational Analysis of Confocal Images

Immunostaining for DNA Modifications: Computational Analysis of Confocal Images

Published on: September 7, 2017

Related Experiment Videos

Last Updated: Dec 25, 2025

An Electrochemiluminescence-Based Assay for MeCP2 Protein Variants

An Electrochemiluminescence-Based Assay for MeCP2 Protein Variants

Published on: May 22, 2020

Repressing Gene Transcription by Redirecting Cellular Machinery with Chemical Epigenetic Modifiers

Repressing Gene Transcription by Redirecting Cellular Machinery with Chemical Epigenetic Modifiers

Published on: September 20, 2018

Immunostaining for DNA Modifications: Computational Analysis of Confocal Images

Immunostaining for DNA Modifications: Computational Analysis of Confocal Images

Published on: September 7, 2017

Area of Science:

Molecular Biology
Neuroscience
Epigenetics

Background:

Methyl-CpG binding protein 2 (MeCP2) is crucial for neuronal development.
MeCP2 recognizes methylated DNA (mCpG) and interacts with regulatory proteins.
Previous studies highlighted ion-dependent discrimination of mCpG and hmCpG by the MeCP2 MBD.

Purpose of the Study:

Investigate the interplay between mCpG/hmCpG recognition by MeCP2's MBD and binding cooperativity.
Determine the influence of ion concentration and type on MeCP2 binding and cooperativity.
Explore the role of polypeptide flexibility in MeCP2 DNA binding.

Main Methods:

Nuclear magnetic resonance (NMR) spectroscopy to analyze MeCP2 structure and ion interactions.
Biophysical assays to study MeCP2 binding affinity and cooperativity under varying ionic conditions.
Investigated effects of protein-stabilizing solutes (TMAO, glutamate) on MeCP2 binding.

Main Results:

MeCP2 binding cooperativity is sensitive to ion concentration and counterions, suppressing DNA modification discrimination.
High ion concentrations abolish cooperativity, indicating electrostatic interactions.
Anion substitution (SO4(2-) for Cl(-)) impacts cooperativity, relevant to neuronal development.
TMAO and glutamate decrease MeCP2 binding affinity but not cooperativity, suggesting polypeptide flexibility is important.
NMR data show ions alter MeCP2 MBD and C-terminal domain structures, affecting residues linked to Rett syndrome.

Conclusions:

MeCP2's DNA binding specificity and cooperativity are modulated by ionic environment and polypeptide flexibility.
These findings offer insights into MeCP2 function in chromatin binding, neuronal function, and development.
Understanding MeCP2's response to ionic changes is critical for comprehending its role in neurological disorders.