Discovery of a chemical probe for the L3MBTL3 methyllysine reader domain View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2013-03

AUTHORS

Lindsey I James, Dalia Barsyte-Lovejoy, Nan Zhong, Liubov Krichevsky, Victoria K Korboukh, J Martin Herold, Christopher J MacNevin, Jacqueline L Norris, Cari A Sagum, Wolfram Tempel, Edyta Marcon, Hongbo Guo, Cen Gao, Xi-Ping Huang, Shili Duan, Andrew Emili, Jack F Greenblatt, Dmitri B Kireev, Jian Jin, William P Janzen, Peter J Brown, Mark T Bedford, Cheryl H Arrowsmith, Stephen V Frye

ABSTRACT

We describe the discovery of UNC1215, a potent and selective chemical probe for the methyllysine (Kme) reading function of L3MBTL3, a member of the malignant brain tumor (MBT) family of chromatin-interacting transcriptional repressors. UNC1215 binds L3MBTL3 with a K(d) of 120 nM, competitively displacing mono- or dimethyllysine-containing peptides, and is greater than 50-fold more potent toward L3MBTL3 than other members of the MBT family while also demonstrating selectivity against more than 200 other reader domains examined. X-ray crystallography identified a unique 2:2 polyvalent mode of interaction between UNC1215 and L3MBTL3. In cells, UNC1215 is nontoxic and directly binds L3MBTL3 via the Kme-binding pocket of the MBT domains. UNC1215 increases the cellular mobility of GFP-L3MBTL3 fusion proteins, and point mutants that disrupt the Kme-binding function of GFP-L3MBTL3 phenocopy the effects of UNC1215 on localization. Finally, UNC1215 was used to reveal a new Kme-dependent interaction of L3MBTL3 with BCLAF1, a protein implicated in DNA damage repair and apoptosis. More... »

PAGES

184

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/nchembio.1157

DOI

http://dx.doi.org/10.1038/nchembio.1157

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1035166329

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/23292653


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