A complex containing N-CoR, mSin3 and histone deacetylase mediates transcriptional repression

被引:1067
作者
Heinzel, T
Lavinsky, RM
Mullen, TM
Soderstrom, M
Laherty, CD
Torchia, J
Yang, WM
Brard, G
Ngo, SD
Davie, JR
Seto, E
Eisenman, RN
Rose, DW
Glass, CK
Rosenfeld, MG
机构
[1] UNIV CALIF SAN DIEGO, HOWARD HUGHES MED INST, LA JOLLA, CA 92093 USA
[2] UNIV CALIF SAN DIEGO, GRAD PROGRAM BIOL, LA JOLLA, CA 92093 USA
[3] UNIV CALIF SAN DIEGO, WHITTIER DIABET PROGRAM, LA JOLLA, CA 92093 USA
[4] UNIV CALIF SAN DIEGO, CELLULAR & MOL MED DEPT, LA JOLLA, CA 92093 USA
[5] UNIV CALIF SAN DIEGO, SCH MED, LA JOLLA, CA 92093 USA
[6] FRED HUTCHINSON CANC RES CTR, DIV BASIC SCI, SEATTLE, WA 98104 USA
[7] UNIV S FLORIDA, DEPT MED MICROBIOL & IMMUNOL, H LEE MOFFIT CANC CTR & RES INST, TAMPA, FL 33612 USA
[8] UNIV MANITOBA, DEPT BIOCHEM & MOL BIOL, WINNIPEG, MB R3E 0W3, CANADA
关键词
D O I
10.1038/387043a0
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Transcriptional repression by nuclear receptors has been correlated to binding of the putative co-repressor, N-CoR, A complex has been identified that contains N-CoR, the Mad presumptive co-repressor mSin3, and the histone deacetylase mRPD3, and which is required for both nuclear receptor- and Mad-dependent repression, but not for repression by transcription factors of the ets-domain family, These data predict that the ligand-induced switch of heterodimeric nuclear receptors from repressor to activator functions involves the exchange of complexes containing histone deacetylases with those that have histone acetylase activity.
引用
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页码:43 / 48
页数:6
相关论文
共 51 条
[1]   HISTONE ACETYLATION INFLUENCES BOTH GENE-EXPRESSION AND DEVELOPMENT OF XENOPUS-LAEVIS [J].
ALMOUZNI, G ;
KHOCHBIN, S ;
DIMITROV, S ;
WOLFFE, AP .
DEVELOPMENTAL BIOLOGY, 1994, 165 (02) :654-669
[2]  
Ayer DE, 1996, MOL CELL BIOL, V16, P5772
[3]   MAD-MAX TRANSCRIPTIONAL REPRESSION IS MEDIATED BY TERNARY COMPLEX-FORMATION WITH MAMMALIAN HOMOLOGS OF YEAST REPRESSOR SIN3 [J].
AYER, DE ;
LAWRENCE, QA ;
EISENMAN, RN .
CELL, 1995, 80 (05) :767-776
[4]   MAD - A HETERODIMERIC PARTNER FOR MAX THAT ANTAGONIZES MYC TRANSCRIPTIONAL ACTIVITY [J].
AYER, DE ;
KRETZNER, L ;
EISENMAN, RN .
CELL, 1993, 72 (02) :211-222
[5]   A SWITCH FROM MYC-MAX TO MAD-MAX HETEROCOMPLEXES ACCOMPANIES MONOCYTE/MACROPHAGE DIFFERENTIATION [J].
AYER, DE ;
EISENMAN, RN .
GENES & DEVELOPMENT, 1993, 7 (11) :2110-2119
[6]   THE TAU-4 ACTIVATION DOMAIN OF THE THYROID-HORMONE RECEPTOR IS REQUIRED FOR RELEASE OF A PUTATIVE COREPRESSOR(S) NECESSARY FOR TRANSCRIPTIONAL SILENCING [J].
BANIAHMAD, A ;
LENG, XH ;
BURRIS, TP ;
TSAI, SY ;
TSAI, MJ ;
OMALLEY, BW .
MOLECULAR AND CELLULAR BIOLOGY, 1995, 15 (01) :76-86
[7]   A TRANSFERABLE SILENCING DOMAIN IS PRESENT IN THE THYROID-HORMONE RECEPTOR, IN THE V-ERBA ONCOGENE PRODUCT AND IN THE RETINOIC ACID RECEPTOR [J].
BANIAHMAD, A ;
KOHNE, AC ;
RENKAWITZ, R .
EMBO JOURNAL, 1992, 11 (03) :1015-1023
[8]   INTERACTION OF HUMAN THYROID-HORMONE RECEPTOR-BETA WITH TRANSCRIPTION FACTOR TFIIB MAY MEDIATE TARGET GENE DEREPRESSION AND ACTIVATION BY THYROID-HORMONE [J].
BANIAHMAD, A ;
HA, I ;
REINBERG, D ;
TSAI, S ;
TSAI, MJ ;
OMALLEY, BW .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1993, 90 (19) :8832-8836
[9]   The CBP co-activator is a histone acetyltransferase [J].
Bannister, AJ ;
Kouzarides, T .
NATURE, 1996, 384 (6610) :641-643
[10]  
Chambon Pierre, 1994, Seminars in Cell Biology, V5, P115, DOI 10.1006/scel.1994.1015