Self-hydroxylation of the splicing factor lysyl hydroxylase, JMJD6

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. 1H-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.

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. 1H-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.

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

SN - 2040-2503

VL - 3

SP - 80

EP - 85

JO - MedChemComm

JF - MedChemComm

IS - 1

ER -