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.

In: MedChemComm, Vol. 3, No. 1, 01.01.2012, p. 80-85.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Mantri, M, Webby, CJ, Loik, ND, Hamed, RB, McDonough, MA, McCullagh, JSO, Schofield, CJ, Wolf, A, Nielsen, ML & Böttger, A 2012, 'Self-hydroxylation of the splicing factor lysyl hydroxylase, JMJD6', MedChemComm, vol. 3, no. 1, pp. 80-85. https://doi.org/10.1039/c1md00225b

APA

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. (2012). Self-hydroxylation of the splicing factor lysyl hydroxylase, JMJD6. MedChemComm, 3(1), 80-85. https://doi.org/10.1039/c1md00225b

Vancouver

Mantri M, Webby CJ, Loik ND, Hamed RB, McDonough MA, McCullagh JSO et al. Self-hydroxylation of the splicing factor lysyl hydroxylase, JMJD6. MedChemComm. 2012 Jan 1;3(1):80-85. https://doi.org/10.1039/c1md00225b

Author

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. / Self-hydroxylation of the splicing factor lysyl hydroxylase, JMJD6. In: MedChemComm. 2012 ; Vol. 3, No. 1. pp. 80-85.

Bibtex

@article{7823a566f6f64777895b96d15e0c1be5,
title = "Self-hydroxylation of the splicing factor lysyl hydroxylase, JMJD6",
abstract = "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",
author = "M. Mantri and C.J. Webby and N.D. Loik and R.B. Hamed and M.A. McDonough and J.S.O. McCullagh and C.J. Schofield and A. Wolf and M.L. Nielsen and A. B{\"o}ttger",
year = "2012",
month = jan,
day = "1",
doi = "10.1039/c1md00225b",
language = "English",
volume = "3",
pages = "80--85",
journal = "MedChemComm",
issn = "2040-2503",
publisher = "Royal Society of Chemistry",
number = "1",

}

RIS

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