Linked Life Data

19799855

Source:http://linkedlifedata.com/resource/pubmed/id/19799855

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2009-10-26
pubmed:abstractText
Recent studies have shown that some Jumonji domain containing proteins demethylate tri- and dimethylated histone lysines by catalyzing a dioxygenase reaction. Here we report the substrate specificity of Jumonji domain-2 family histone demethylases (JMJD2A-C). A candidate substrate-based approach demonstrated that in addition to its known substrate, trimethylated histone H3-lysine-9, JMJD2A-C demethylate trimethylated lysine containing peptides from WIZ, CDYL1, CSB and G9a proteins, all constituents of transcription repression complexes. Our results are consistent with lax substrate specificities observed for the iron (II), 2-oxoglutarate-dependent dioxygenases, and shed new light on signaling pathways regulated by Jumonji domain-2 family histone demethylases during epigenetic transcriptional regulation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
1090-2104
pubmed:author
pubmed:issnType
Electronic
pubmed:day
11
pubmed:volume
390
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
280-4
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Identification of non-histone substrates for JMJD2A-C histone demethylases.
pubmed:affiliation
Division of Pharmaceutical Sciences, School of Pharmacy, University of Missouri-Kansas City, Kansas City, MO 64108-2718, USA.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't