Linked Life Data

20194436

Source:http://linkedlifedata.com/resource/pubmed/id/20194436

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2010-3-2
pubmed:abstractText
Methylation of histone H3 Lys 9 and Lys 27 (H3K9 and H3K27) is associated with transcriptional silencing. Here we show that KDM7, a JmjC domain-containing protein, catalyzes demethylation of both mono- or dimethylated H3K9 and H3K27. Inhibition of KDM7 orthologs in zebrafish resulted in developmental brain defects. KDM7 interacts with the follistatin gene locus, and KDM7 depletion in mammalian neuronal cells suppressed follistatin gene transcription in association with increased levels of dimethylated H3K9 and H3K27. Our findings identify KDM7 as a dual demethylase for H3K9 and H3K27 that functions as an eraser of silencing marks on chromatin during brain development.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
1549-5477
pubmed:author
pubmed:issnType
Electronic
pubmed:day
1
pubmed:volume
24
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
432-7
pubmed:dateRevised
2010-9-2
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
KDM7 is a dual demethylase for histone H3 Lys 9 and Lys 27 and functions in brain development.
pubmed:affiliation
Medical Institute of Bioregulation, Kyushu University, Higashi-ku, Fukuoka, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't