Histone deacetylase 3 is selectively involved in L3MBTL2-mediated transcriptional repression.
This is the first report that L(3)mbt-like 2 (L3MBTL2) specifically interacts with the histone deacetylase domain of histone deacetylase 3 (HDAC3) via its MBT domain. Here, we show that L3MBTL2 selectively interacts with HDAC3, but not other class I HDACs. An in vitro peptide-binding assay demonstrated the specific association of HDAC3 with methylated histone-K20 tail and L3MBTL2. Furthermore, depletion of HDAC3 resulted in a decrease of methylated K20-H4, as well as an increase in acetylated histone H3. Consequently, HDAC3 knock-down selectively suppressed L3MBTL2-mediated transcriptional repression. Taken together, our results reveal the concerted action of both HDAC3 and L3MBTL2 in histone deacetylation and methylation-dependent transcriptional repression.
Yoo
Jung-Yoon
JY
Department of Biochemistry and Molecular Biology, Institute of Genetic Science, Yonsei University College of Medicine, South Korea.
Choi
Kyung-Chul
KC
Kang
HeeBum
H
Kim
Young Jun
YJ
Lee
Jeongmin
J
Jun
Woo Jin
WJ
Kim
Mi-Jeong
MJ
Lee
Yoo-Hyun
YH
Lee
Ok-Hee
OH
Yoon
Ho-Geun
HG
D000818:Animals; D015870:Gene Expression; D006655:Histone Deacetylases / Q000235:genetics* / Q000378:metabolism; D006657:Histones / Q000235:genetics*; D000099186:Histone Deacetylase 3
D006655:Histone Deacetylases; D006657:Histones; D000099186:Histone Deacetylase 3