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Profiling of Methyltransferases and Other S-adenosyl-L-homocysteine-binding Proteins by Capture Compound Mass Spectrometry CCMS

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Profiling Cytidine Acetylation with Specific Affinity and Reactivity.

Wilson R Sinclair¹, Daniel Arango², Jonathan H Shrimp¹

¹Chemical Biology Laboratory, Center for Cancer Research, National Cancer Institute, National Institutes of Health , Frederick, Maryland 21702, United States.

ACS Chemical Biology

|October 18, 2017

Summary

This summary is machine-generated.

Researchers developed chemical methods to study N4-acetylcytidine (ac4C), a key RNA modification. These tools enable antibody screening and accurately track ac4C in cells, advancing epitranscriptomics research.

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Selective Capture of 5-hydroxymethylcytosine from Genomic DNA

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Last Updated: Feb 20, 2026

Profiling of Methyltransferases and Other S-adenosyl-L-homocysteine-binding Proteins by Capture Compound Mass Spectrometry CCMS

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Efficient Purification and LC-MS/MS-based Assay Development for Ten-Eleven Translocation-2 5-Methylcytosine Dioxygenase

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Published on: October 15, 2018

Selective Capture of 5-hydroxymethylcytosine from Genomic DNA

Selective Capture of 5-hydroxymethylcytosine from Genomic DNA

Published on: October 5, 2012

Area of Science:

Biochemistry
Molecular Biology
Chemical Biology

Background:

The human acetyltransferase NAT10 catalyzes the formation of N4-acetylcytidine (ac4C), a crucial RNA modification impacting RNA structure and function.
Understanding the biological roles and disease relevance of RNA acetyltransferases and modifications like ac4C is essential.

Purpose of the Study:

To develop and apply novel chemical methods for studying ac4C modifications in biological systems.
To create tools for screening and validating affinity reagents targeting ac4C.

Main Methods:

Conjugation of ac4C to carrier proteins using optimized chemical protocols.
Development of methods to isolate ac4C-containing RNAs for antibody screening.
Validation of ac4C affinity reagent specificity using chemical deacetylation assays in cellular RNA.

Main Results:

Successfully conjugated ac4C to carrier proteins, enabling antibody production.
Established protocols for accessing ac4C-modified RNAs, facilitating antibody screening.
Validated an ac4C affinity reagent's specificity and accuracy in detecting ac4C in cellular contexts.

Conclusions:

The developed chemical methods provide powerful tools for studying ac4C modifications and their biological roles.
These tools offer new insights into the stability and half-life of the conserved ac4C RNA modification.
Chemical reactivity can be leveraged to create and validate affinity reagents for the emerging field of epitranscriptomics.