TY - JOUR
T1 - RNA-dependent chromatin localization of KDM4D lysine demethylase promotes H3K9me3 demethylation
AU - Zoabi, Muhammad
AU - Nadar-Ponniah, Prathamesh T.
AU - Khoury-Haddad, Hanan
AU - Usaj, Marko
AU - Budowski-Tal, Inbal
AU - Haran, Tali
AU - Henn, Arnon
AU - Mandel-Gutfreund, Yael
AU - Ayoub, Nabieh
N1 - Funding Information: Israel Cancer Research Fund (ICRF) [2015211]; Israel Science Foundation [2014673]; the Israel Cancer association [2019404]; the H. Blechman and Eliayu Pen Memorial Cancer Research Fund [2018025]. Funding for open access charge: Israel Cancer Research Fund (ICRF); Israel Science Foundation; the Israel Cancer association; the H. Blechman and Eliayu Pen Memorial Cancer Research Fund. Conflict of interest statement. None declared. Publisher Copyright: © 2014 The Author(s).
PY - 2014/12/1
Y1 - 2014/12/1
N2 - The JmjC-containing lysine demethylase, KDM4D, demethylates di-and tri-methylation of histone H3 on lysine 9 (H3K9me3). How KDM4D is recruited to chromatin and recognizes its histone substrates remains unknown. Here, we show that KDM4D binds RNA independently of its demethylase activity. We mapped two non-canonical RNA binding domains: the first is within the N-terminal spanning amino acids 115 to 236, and the second is within the C-terminal spanning amino acids 348 to 523 of KDM4D. We also demonstrate that RNA interactions with KDM4D N-terminal region are critical for its association with chromatin and subsequently for demethylating H3K9me3 in cells. This study implicates, for the first time, RNA molecules in regulating the levels of H3K9 methylation by affecting KDM4D association with chromatin.
AB - The JmjC-containing lysine demethylase, KDM4D, demethylates di-and tri-methylation of histone H3 on lysine 9 (H3K9me3). How KDM4D is recruited to chromatin and recognizes its histone substrates remains unknown. Here, we show that KDM4D binds RNA independently of its demethylase activity. We mapped two non-canonical RNA binding domains: the first is within the N-terminal spanning amino acids 115 to 236, and the second is within the C-terminal spanning amino acids 348 to 523 of KDM4D. We also demonstrate that RNA interactions with KDM4D N-terminal region are critical for its association with chromatin and subsequently for demethylating H3K9me3 in cells. This study implicates, for the first time, RNA molecules in regulating the levels of H3K9 methylation by affecting KDM4D association with chromatin.
UR - https://www.mendeley.com/catalogue/9aefa016-30d1-3f23-aa41-606f94c28a42/
UR - http://www.scopus.com/inward/record.url?scp=84941128274&partnerID=8YFLogxK
U2 - https://doi.org/10.1093/nar/gku1021
DO - https://doi.org/10.1093/nar/gku1021
M3 - Article
C2 - 25378304
SN - 0305-1048
VL - 42
SP - 13026
EP - 13038
JO - Nucleic acids research
JF - Nucleic acids research
IS - 21
ER -