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The Jumonji-C oxygenase JMJD7 catalyzes (3S)-lysyl hydroxylation of TRAFAC GTPases

Abstract:

Biochemical, structural, and cellular studies reveal Jumonji-C (JmjC) domain-containing 7 (JMJD7) as a 2-oxoglutarate (2OG)-dependent oxygenase catalyzing a previously unreported type of post translational modification, (3S)-lysyl hydroxylation. Crystallographic analyses reveal JMJD7 as more closely related to the JmjC hydroxylases rather than the JmjC demethylases. Biophysical and mutation studies show that JMJD7 has a unique dimerization mode, with interactions between monomers involvin...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1038/s41589-018-0071-y

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Institution:
University of Oxford
Division:
MPLS Division
Department:
Chemistry; Organic Chemistry
Role:
Author
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Institution:
University of Oxford
Division:
MPLS Division
Department:
Chemistry
Role:
Author
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Funding agency for:
Markolovic, S
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Funding agency for:
Abboud, MI
Grant:
Junior Research Fellowship
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Funding agency for:
Schofield, CJ
Grant:
106244/Z/14/Z
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Funding agency for:
Schofield, CJ
Grant:
106244/Z/14/Z
Publisher:
Springer Nature Publisher's website
Journal:
Nature Chemical Biology Journal website
Volume:
14
Pages:
688–695
Publication date:
2018-06-18
Acceptance date:
2018-04-09
DOI:
EISSN:
1552-4469
ISSN:
1552-4450
Source identifiers:
835039
Pubs id:
pubs:835039
UUID:
uuid:62b9cef7-9260-4913-8914-346bd0d166bf
Local pid:
pubs:835039
Deposit date:
2018-04-11

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