TY - JOUR
T1 - Histone H3 lysine 36 dimethylation (H3K36me2) is sufficient to recruit the Rpd3s Histone deacetylase complex and to repress spurious transcription
AU - Li, Bing
AU - Jackson, Jessica
AU - Simon, Matthew D.
AU - Fleharty, Brian
AU - Gogol, Madelaine
AU - Seidel, Chris
AU - Workman, Jerry L.
AU - Shilatifard, Ali
PY - 2009/3/20
Y1 - 2009/3/20
N2 - Histone methylation is associated with both transcription activation and repression. However, the functions of different states of methylation remain largely elusive. Here, using methyllysine analog technology, we demonstrate that the histone deacetylase complex, Rpd3S, can distinguish the nucleosomes methylated to different extents and that K36me2 is sufficient to target Rpd3S in vitro. Through a genome-wide survey, we identified a few mutants in which the level of K36me3 is significantly reduced, whereas the level of K36me2 is sustained. Transcription analysis and genome-wide histone modification studies on these mutants suggested that K36me2 is sufficient to target Rpd3S in vivo, thereby maintaining a functional Set2-Rpd3S pathway.
AB - Histone methylation is associated with both transcription activation and repression. However, the functions of different states of methylation remain largely elusive. Here, using methyllysine analog technology, we demonstrate that the histone deacetylase complex, Rpd3S, can distinguish the nucleosomes methylated to different extents and that K36me2 is sufficient to target Rpd3S in vitro. Through a genome-wide survey, we identified a few mutants in which the level of K36me3 is significantly reduced, whereas the level of K36me2 is sustained. Transcription analysis and genome-wide histone modification studies on these mutants suggested that K36me2 is sufficient to target Rpd3S in vivo, thereby maintaining a functional Set2-Rpd3S pathway.
UR - http://www.scopus.com/inward/record.url?scp=65549095078&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=65549095078&partnerID=8YFLogxK
U2 - 10.1074/jbc.M808220200
DO - 10.1074/jbc.M808220200
M3 - Article
C2 - 19155214
AN - SCOPUS:65549095078
SN - 0021-9258
VL - 284
SP - 7970
EP - 7976
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 12
ER -