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Böttger, A.* ; Islam, M.S.* ; Chowdhury, R.* ; Schofield, C.J.* ; Wolf, A.

The oxygenase Jmjd6-a case study in conflicting assignments.

Biochem. J. 468, 191-202 (2015)
DOI PMC
Open Access Green möglich sobald Postprint bei der ZB eingereicht worden ist.
The Jumonji domain-containing protein 6 (Jmjd6) is a member of the superfamily of non-haem iron(II) and 2-oxoglutarate (2OG)-dependent oxygenases; it plays an important developmental role in higher animals. Jmjd6 was initially assigned a role as the phosphatidylserine receptor responsible for engulfment of apoptotic cells but this now seems unlikely. Jmjd6 has been shown to be a nuclear localized protein with a JmjC domain comprising a distorted double-stranded β-helical structure characteristic of the 2OG-dependent oxygenases. Jmjd6 was subsequently assigned a role in catalysing N-methyl-arginine residue demethylation on the N-terminus of the human histones H3 and H4; however, this function is also subject to conflicting reports. Jmjd6 does catalyse 2OG-dependent C-5 hydroxylation of lysine residues in mRNA splicing-regulatory proteins and histones; there is also accumulating evidence that Jmjd6 plays a role in splicing (potentially in an iron- and oxygen-dependent manner) as well as in other processes regulating gene expression, including transcriptional pause release. Moreover, a link with tumour progression has been suggested. In the present review we look at biochemical, structural and cellular work on Jmjd6, highlighting areas of controversy and consensus.
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Publikationstyp Artikel: Journalartikel
Dokumenttyp Review
Korrespondenzautor
Schlagwörter Alternative Splicing ; Arginine-demethylase ; Epigenetic Regulation ; Fe(ii) And 2-oxoglutarate Dependent Oxygenases ; Hydroxylysine ; Jmjc ; Jmjd6 ; Jumonji ; Lysine-hydroxylase ; Sr-proteins; Hypoxia-inducible Factor; Bromodomain Protein Brd4; Inhibiting-hif Fih; Vegf-receptor 1; Phosphatidylserine Receptor; Apoptotic Cells; 2-oxoglutarate Oxygenases; Lysyl Hydroxylase; Asparaginyl Hydroxylase; P-tefb
ISSN (print) / ISBN 0264-6021
e-ISSN 1470-8728
Zeitschrift Biochemical Journal / Reviews
Quellenangaben Band: 468, Heft: 2, Seiten: 191-202 Artikelnummer: , Supplement: ,
Verlag Portland Press
Verlagsort London
Nichtpatentliteratur Publikationen
Begutachtungsstatus Peer reviewed
Institut(e) Institute of Molecular Toxicology and Pharmacology (TOXI)