Tracking DOT1L methyltransferase activity by stable isotope labelling using a selective synthetic co-factor
Epigenetic processes influence health and disease through mechanisms which alter gene expression. In contrast to genetic changes which affect DNA sequences, epigenetic marks include DNA base modifications or post-translational modification (PTM) of proteins. Histone methylation is a prominent and ve...
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| Published in | Communications chemistry Vol. 7; no. 1; pp. 145 - 7 |
|---|---|
| Main Authors | , , , , , , |
| Format | Journal Article |
| Language | English |
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London
Nature Publishing Group UK
27.06.2024
Nature Publishing Group Nature Portfolio |
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| Abstract | Epigenetic processes influence health and disease through mechanisms which alter gene expression. In contrast to genetic changes which affect DNA sequences, epigenetic marks include DNA base modifications or post-translational modification (PTM) of proteins. Histone methylation is a prominent and versatile example of an epigenetic marker: gene expression or silencing is dependent on the location and extent of the methylation. Protein methyltransferases exhibit functional redundancy and broad preferences for multiple histone residues, which presents a challenge for the study of their individual activities. We developed an isotopically labelled analogue of co-factor S-adenosyl-L-methionine (
13
CD
3
-BrSAM), with selectivity for the histone lysine methyltransferase DOT1L, permitting tracking of methylation activity by mass spectrometry (MS). This concept could be applied to other methyltransferases, linking PTM discovery to enzymatic mediators.
Histone methylation by histone lysine methyltransferases (HKMTs) is a vital post-translational modification regulating gene expression, however, selective mapping of methylation by proteomics analysis remains challenging. Here, the authors develop a heavy co-factor analogue
13
CD
3
-BrSAM for HKMT DOT1L that can selectively heavy label target substrates, and map their methylation by proteomics. |
|---|---|
| AbstractList | Epigenetic processes influence health and disease through mechanisms which alter gene expression. In contrast to genetic changes which affect DNA sequences, epigenetic marks include DNA base modifications or post-translational modification (PTM) of proteins. Histone methylation is a prominent and versatile example of an epigenetic marker: gene expression or silencing is dependent on the location and extent of the methylation. Protein methyltransferases exhibit functional redundancy and broad preferences for multiple histone residues, which presents a challenge for the study of their individual activities. We developed an isotopically labelled analogue of co-factor S-adenosyl-L-methionine (13CD3-BrSAM), with selectivity for the histone lysine methyltransferase DOT1L, permitting tracking of methylation activity by mass spectrometry (MS). This concept could be applied to other methyltransferases, linking PTM discovery to enzymatic mediators.Histone methylation by histone lysine methyltransferases (HKMTs) is a vital post-translational modification regulating gene expression, however, selective mapping of methylation by proteomics analysis remains challenging. Here, the authors develop a heavy co-factor analogue 13CD3-BrSAM for HKMT DOT1L that can selectively heavy label target substrates, and map their methylation by proteomics. Epigenetic processes influence health and disease through mechanisms which alter gene expression. In contrast to genetic changes which affect DNA sequences, epigenetic marks include DNA base modifications or post-translational modification (PTM) of proteins. Histone methylation is a prominent and versatile example of an epigenetic marker: gene expression or silencing is dependent on the location and extent of the methylation. Protein methyltransferases exhibit functional redundancy and broad preferences for multiple histone residues, which presents a challenge for the study of their individual activities. We developed an isotopically labelled analogue of co-factor S-adenosyl-L-methionine ( 13 CD 3 -BrSAM), with selectivity for the histone lysine methyltransferase DOT1L, permitting tracking of methylation activity by mass spectrometry (MS). This concept could be applied to other methyltransferases, linking PTM discovery to enzymatic mediators. Abstract Epigenetic processes influence health and disease through mechanisms which alter gene expression. In contrast to genetic changes which affect DNA sequences, epigenetic marks include DNA base modifications or post-translational modification (PTM) of proteins. Histone methylation is a prominent and versatile example of an epigenetic marker: gene expression or silencing is dependent on the location and extent of the methylation. Protein methyltransferases exhibit functional redundancy and broad preferences for multiple histone residues, which presents a challenge for the study of their individual activities. We developed an isotopically labelled analogue of co-factor S-adenosyl-L-methionine (13CD3-BrSAM), with selectivity for the histone lysine methyltransferase DOT1L, permitting tracking of methylation activity by mass spectrometry (MS). This concept could be applied to other methyltransferases, linking PTM discovery to enzymatic mediators. Epigenetic processes influence health and disease through mechanisms which alter gene expression. In contrast to genetic changes which affect DNA sequences, epigenetic marks include DNA base modifications or post-translational modification (PTM) of proteins. Histone methylation is a prominent and versatile example of an epigenetic marker: gene expression or silencing is dependent on the location and extent of the methylation. Protein methyltransferases exhibit functional redundancy and broad preferences for multiple histone residues, which presents a challenge for the study of their individual activities. We developed an isotopically labelled analogue of co-factor S-adenosyl-L-methionine ( 13 CD 3 -BrSAM), with selectivity for the histone lysine methyltransferase DOT1L, permitting tracking of methylation activity by mass spectrometry (MS). This concept could be applied to other methyltransferases, linking PTM discovery to enzymatic mediators. Histone methylation by histone lysine methyltransferases (HKMTs) is a vital post-translational modification regulating gene expression, however, selective mapping of methylation by proteomics analysis remains challenging. Here, the authors develop a heavy co-factor analogue 13 CD 3 -BrSAM for HKMT DOT1L that can selectively heavy label target substrates, and map their methylation by proteomics. Epigenetic processes influence health and disease through mechanisms which alter gene expression. In contrast to genetic changes which affect DNA sequences, epigenetic marks include DNA base modifications or post-translational modification (PTM) of proteins. Histone methylation is a prominent and versatile example of an epigenetic marker: gene expression or silencing is dependent on the location and extent of the methylation. Protein methyltransferases exhibit functional redundancy and broad preferences for multiple histone residues, which presents a challenge for the study of their individual activities. We developed an isotopically labelled analogue of co-factor S-adenosyl-L-methionine (13CD3-BrSAM), with selectivity for the histone lysine methyltransferase DOT1L, permitting tracking of methylation activity by mass spectrometry (MS). This concept could be applied to other methyltransferases, linking PTM discovery to enzymatic mediators.Epigenetic processes influence health and disease through mechanisms which alter gene expression. In contrast to genetic changes which affect DNA sequences, epigenetic marks include DNA base modifications or post-translational modification (PTM) of proteins. Histone methylation is a prominent and versatile example of an epigenetic marker: gene expression or silencing is dependent on the location and extent of the methylation. Protein methyltransferases exhibit functional redundancy and broad preferences for multiple histone residues, which presents a challenge for the study of their individual activities. We developed an isotopically labelled analogue of co-factor S-adenosyl-L-methionine (13CD3-BrSAM), with selectivity for the histone lysine methyltransferase DOT1L, permitting tracking of methylation activity by mass spectrometry (MS). This concept could be applied to other methyltransferases, linking PTM discovery to enzymatic mediators. Epigenetic processes influence health and disease through mechanisms which alter gene expression. In contrast to genetic changes which affect DNA sequences, epigenetic marks include DNA base modifications or post-translational modification (PTM) of proteins. Histone methylation is a prominent and versatile example of an epigenetic marker: gene expression or silencing is dependent on the location and extent of the methylation. Protein methyltransferases exhibit functional redundancy and broad preferences for multiple histone residues, which presents a challenge for the study of their individual activities. We developed an isotopically labelled analogue of co-factor S-adenosyl-L-methionine ( CD -BrSAM), with selectivity for the histone lysine methyltransferase DOT1L, permitting tracking of methylation activity by mass spectrometry (MS). This concept could be applied to other methyltransferases, linking PTM discovery to enzymatic mediators. |
| ArticleNumber | 145 |
| Author | Whitwell, Harry J. Jiménez, Beatriz Fuchter, Matthew J. Trainor, Nicole Leonidou, Emily Addison, Katie DiMaggio, Peter A. |
| Author_xml | – sequence: 1 givenname: Nicole orcidid: 0000-0002-3758-9969 surname: Trainor fullname: Trainor, Nicole organization: Department of Chemistry, Molecular Sciences Research Hub, Imperial College London, White City Campus – sequence: 2 givenname: Harry J. surname: Whitwell fullname: Whitwell, Harry J. organization: National Phenome Centre and Imperial Clinical Phenotyping Centre, Department of Metabolism, Digestion and Reproduction, IRDB, Building Imperial College London, Section of Bioanalytical Chemistry, Division of Systems Medicine, Department of Metabolism, Digestion and Reproduction, Sir Alexander Fleming Building, Imperial College London – sequence: 3 givenname: Beatriz surname: Jiménez fullname: Jiménez, Beatriz organization: National Phenome Centre and Imperial Clinical Phenotyping Centre, Department of Metabolism, Digestion and Reproduction, IRDB, Building Imperial College London, Section of Bioanalytical Chemistry, Division of Systems Medicine, Department of Metabolism, Digestion and Reproduction, Sir Alexander Fleming Building, Imperial College London – sequence: 4 givenname: Katie surname: Addison fullname: Addison, Katie organization: Department of Chemistry, Molecular Sciences Research Hub, Imperial College London, White City Campus – sequence: 5 givenname: Emily surname: Leonidou fullname: Leonidou, Emily organization: Department of Chemistry, Molecular Sciences Research Hub, Imperial College London, White City Campus, Department of Chemical Engineering, Imperial College London, South Kensington Campus – sequence: 6 givenname: Peter A. surname: DiMaggio fullname: DiMaggio, Peter A. organization: Department of Chemical Engineering, Imperial College London, South Kensington Campus – sequence: 7 givenname: Matthew J. orcidid: 0000-0002-1767-7072 surname: Fuchter fullname: Fuchter, Matthew J. email: m.fuchter@imperial.ac.uk organization: Department of Chemistry, Molecular Sciences Research Hub, Imperial College London, White City Campus |
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| Title | Tracking DOT1L methyltransferase activity by stable isotope labelling using a selective synthetic co-factor |
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