Self-hydroxylation of the splicing factor lysyl hydroxylase, JMJD6
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Self-hydroxylation of the splicing factor lysyl hydroxylase, JMJD6. / Mantri, M.; Webby, C.J.; Loik, N.D.; Hamed, R.B.; McDonough, M.A.; McCullagh, J.S.O.; Schofield, C.J.; Wolf, A.; Nielsen, M.L.; Böttger, A.
I: MedChemComm, Bind 3, Nr. 1, 01.01.2012, s. 80-85.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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TY - JOUR
T1 - Self-hydroxylation of the splicing factor lysyl hydroxylase, JMJD6
AU - Mantri, M.
AU - Webby, C.J.
AU - Loik, N.D.
AU - Hamed, R.B.
AU - McDonough, M.A.
AU - McCullagh, J.S.O.
AU - Schofield, C.J.
AU - Wolf, A.
AU - Nielsen, M.L.
AU - Böttger, A.
PY - 2012/1/1
Y1 - 2012/1/1
N2 - The lysyl 5S-hydroxylase, JMJD6 acts on proteins involved in RNA splicing. We find that in the absence of substrate JMJD6 catalyses turnover of 2OG to succinate. H-NMR analyses demonstrate that consumption of 2OG is coupled to succinate formation. MS analyses reveal that JMJD6 undergoes self-hydroxylation in the presence of Fe(ii) and 2OG resulting in production of 5S-hydroxylysine residues. JMJD6 in human cells is also found to be hydroxylated. Self-hydroxylation of JMJD6 may play a regulatory role in modulating the hydroxylation status of proteins involved in RNA splicing. This journal is
AB - The lysyl 5S-hydroxylase, JMJD6 acts on proteins involved in RNA splicing. We find that in the absence of substrate JMJD6 catalyses turnover of 2OG to succinate. H-NMR analyses demonstrate that consumption of 2OG is coupled to succinate formation. MS analyses reveal that JMJD6 undergoes self-hydroxylation in the presence of Fe(ii) and 2OG resulting in production of 5S-hydroxylysine residues. JMJD6 in human cells is also found to be hydroxylated. Self-hydroxylation of JMJD6 may play a regulatory role in modulating the hydroxylation status of proteins involved in RNA splicing. This journal is
UR - http://www.scopus.com/inward/record.url?scp=84855692560&partnerID=8YFLogxK
U2 - 10.1039/c1md00225b
DO - 10.1039/c1md00225b
M3 - Journal article
AN - SCOPUS:84855692560
VL - 3
SP - 80
EP - 85
JO - MedChemComm
JF - MedChemComm
SN - 2040-2503
IS - 1
ER -
ID: 46455720