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Mechanistic and structural studies of KDM‐catalysed demethylation of histone 1 isotype 4 at lysine 26

Abstract:

N‐Methylation of lysyl residues is widely observed on histone proteins. Using isolated enzymes, we report mechanistic and structural studies on histone lysine demethylase (KDM)‐catalysed demethylation of Nε‐methylated lysine 26 on histone 1 isotype 4 (H1.4). The results reveal that methylated H1.4K26 is a substrate for all members of the KDM4 subfamily and that KDM4A‐catalysed demethylation of H1.4K26me3 peptide is similarly efficient to that of H3K9me3. Crystallographic studies of an H1.4K26...

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Publication status:
Published
Peer review status:
Peer reviewed
Version:
Publisher's version

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Publisher copy:
10.1002/1873-3468.13231

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Institution:
University of Oxford
Division:
MPLS Division
Department:
Chemistry
Subgroup:
Organic Chemistry
Hopkinson, RJ More by this author
Chowdhury, R More by this author
More by this author
Institution:
University of Oxford
Division:
MPLS Division
Department:
Chemistry
Subgroup:
Organic Chemistry
More by this author
Institution:
University of Oxford
Division:
MPLS Division
Department:
Chemistry
Subgroup:
Organic Chemistry
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Funding agency for:
Walport, LJ
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Funding agency for:
Kawamura, A
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Publisher:
Wiley Publisher's website
Journal:
FEBS Letters Journal website
Volume:
592
Issue:
19
Pages:
3264-3273
Publication date:
2018-09-14
Acceptance date:
2018-08-24
DOI:
ISSN:
1873-3468
Pubs id:
pubs:911001
URN:
uri:90f1eb40-a1e7-46cb-a957-34a48d9ebbaa
UUID:
uuid:90f1eb40-a1e7-46cb-a957-34a48d9ebbaa
Local pid:
pubs:911001

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