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Towards the structural characterization of the human methyltransferome
Michael K Fenwick1, Steven E Ealick1
1Department of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853, United States.
Current Opinion in Structural Biology
|April 15, 2018
Summary
Methyltransferases (MTases) are crucial enzymes, but many are inefficient alone. New structural insights reveal how these methyltransferases are activated through protein interactions, offering a deeper understanding of the human methyltransferome.
Area of Science:
- Biochemistry
- Structural Biology
- Genetics
Background:
- Over 2000 methyltransferase (MTase) structures are known, revealing diverse folds for methyl donor binding.
- Many MTases involved in gene regulation are catalytically inefficient in isolation, with inhibitory active site architectures.
- Recent structural studies of MTase complexes provide insights into biological context and activation mechanisms.
Purpose of the Study:
- To review the structural landscape of the human methyltransferome.
- To elucidate newly discovered structural mechanisms underlying MTase activation.
Main Methods:
- Structural analysis of available methyltransferase (MTase) structures.
- Review of recent crystallographic and cryo-EM studies of MTase complexes.
- Integration of structural data with functional and biological context.
Main Results:
- Fifteen distinct MTase folds have been identified, offering molecular insights into the human methyltransferome.
- Isolated MTases often exhibit inefficient catalysis due to inhibitory active site structures.
- Allosteric activation mechanisms involving histone modifications, reader domains, reader proteins, and activator proteins have been revealed for various MTases.
Conclusions:
- Structural biology is crucial for understanding methyltransferase (MTase) function and regulation.
- Activation mechanisms involving protein-protein interactions are key to overcoming the inherent inefficiency of many MTases.
- These findings advance our knowledge of the human methyltransferome and its regulation in biological processes.
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