Arginine demethylation is catalysed by a subset of JmjC histone lysine demethylases
While reversal of lysine methylation on histone tails is a well-established mechanism to tune gene expression, the existence of a similar arginine demethylation process is controversial. Here, the authors show that some jumonji enzymes possess both lysine and arginine demethylase activity in vitro.
Enregistré dans:
| Auteurs principaux: | , , , , , , |
|---|---|
| Format: | article |
| Langue: | EN |
| Publié: |
Nature Portfolio
2016
|
| Sujets: | |
| Accès en ligne: | https://doaj.org/article/b3dc6971dc6349f5a32b481bb23ad534 |
| Tags: |
Ajouter un tag
Pas de tags, Soyez le premier à ajouter un tag!
|
| id |
oai:doaj.org-article:b3dc6971dc6349f5a32b481bb23ad534 |
|---|---|
| record_format |
dspace |
| spelling |
oai:doaj.org-article:b3dc6971dc6349f5a32b481bb23ad5342021-12-02T15:34:10ZArginine demethylation is catalysed by a subset of JmjC histone lysine demethylases10.1038/ncomms119742041-1723https://doaj.org/article/b3dc6971dc6349f5a32b481bb23ad5342016-06-01T00:00:00Zhttps://doi.org/10.1038/ncomms11974https://doaj.org/toc/2041-1723While reversal of lysine methylation on histone tails is a well-established mechanism to tune gene expression, the existence of a similar arginine demethylation process is controversial. Here, the authors show that some jumonji enzymes possess both lysine and arginine demethylase activity in vitro.Louise J. WalportRichard J. HopkinsonRasheduzzaman ChowdhuryRachel SchillerWei GeAkane KawamuraChristopher J. SchofieldNature PortfolioarticleScienceQENNature Communications, Vol 7, Iss 1, Pp 1-12 (2016) |
| institution |
DOAJ |
| collection |
DOAJ |
| language |
EN |
| topic |
Science Q |
| spellingShingle |
Science Q Louise J. Walport Richard J. Hopkinson Rasheduzzaman Chowdhury Rachel Schiller Wei Ge Akane Kawamura Christopher J. Schofield Arginine demethylation is catalysed by a subset of JmjC histone lysine demethylases |
| description |
While reversal of lysine methylation on histone tails is a well-established mechanism to tune gene expression, the existence of a similar arginine demethylation process is controversial. Here, the authors show that some jumonji enzymes possess both lysine and arginine demethylase activity in vitro. |
| format |
article |
| author |
Louise J. Walport Richard J. Hopkinson Rasheduzzaman Chowdhury Rachel Schiller Wei Ge Akane Kawamura Christopher J. Schofield |
| author_facet |
Louise J. Walport Richard J. Hopkinson Rasheduzzaman Chowdhury Rachel Schiller Wei Ge Akane Kawamura Christopher J. Schofield |
| author_sort |
Louise J. Walport |
| title |
Arginine demethylation is catalysed by a subset of JmjC histone lysine demethylases |
| title_short |
Arginine demethylation is catalysed by a subset of JmjC histone lysine demethylases |
| title_full |
Arginine demethylation is catalysed by a subset of JmjC histone lysine demethylases |
| title_fullStr |
Arginine demethylation is catalysed by a subset of JmjC histone lysine demethylases |
| title_full_unstemmed |
Arginine demethylation is catalysed by a subset of JmjC histone lysine demethylases |
| title_sort |
arginine demethylation is catalysed by a subset of jmjc histone lysine demethylases |
| publisher |
Nature Portfolio |
| publishDate |
2016 |
| url |
https://doaj.org/article/b3dc6971dc6349f5a32b481bb23ad534 |
| work_keys_str_mv |
AT louisejwalport argininedemethylationiscatalysedbyasubsetofjmjchistonelysinedemethylases AT richardjhopkinson argininedemethylationiscatalysedbyasubsetofjmjchistonelysinedemethylases AT rasheduzzamanchowdhury argininedemethylationiscatalysedbyasubsetofjmjchistonelysinedemethylases AT rachelschiller argininedemethylationiscatalysedbyasubsetofjmjchistonelysinedemethylases AT weige argininedemethylationiscatalysedbyasubsetofjmjchistonelysinedemethylases AT akanekawamura argininedemethylationiscatalysedbyasubsetofjmjchistonelysinedemethylases AT christopherjschofield argininedemethylationiscatalysedbyasubsetofjmjchistonelysinedemethylases |
| _version_ |
1718386922655580160 |