Acetylation of histones and transcription-related factors

被引:1375
作者
Sterner, DE [1 ]
Berger, SL [1 ]
机构
[1] Wistar Inst Anat & Biol, Philadelphia, PA 19104 USA
关键词
D O I
10.1128/MMBR.64.2.435-459.2000
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
The state of chromatin (the packaging of DNA in eukaryotes) has long been recognized to have major effects on levels of gene expression, and numerous chromatin-altering strategies-including ATP-dependent remodeling and histone modification-are employed in the cell to bring about transcriptional regulation. Of these, histone acetylation is one of the best characterized, as recent years have seen the identification and further study of many histone acetyltransferase (HAT) proteins and their associated complexes. Interestingly, most of these proteins were previously shown to have coactivator or other transcription-related functions. Confirmed and putative HAT proteins have been identified from various organisms from yeast to humans, and they include Gcn5-related N-acetyltransferase (GNAT) superfamily members Gcn5, PCAF, Elp3, Hpa2 and Hat1: MYSTproteins Sas2, Sas3, Esa1, MOF, Tip60, MOZ, MORF, and HBO1; global coactivators p300 and CREB-binding protein; nuclear receptor coactivators SRC-1, ACTR, and TIF2; TATA-binding protein-associated factor TAF(II)250 and its homologs; and subunits of RNA polymerase III general factor TFIIIC. The acetylation and transcriptional functions of these HATs and the native complexes containing them (such as yeast SAGA, NuA4, and possibly analogous human complexes) are discussed. In addition some of these HA Ts are also known to modify certain nonhistone transcription-related proteins, including high-mobility-group chromatin proteins activators such as p53, coactivators, and general factors. Thus, we also detail these known factor acetyltransferase (FAT) substrates and the demonstrated or potential roles of their acetylation in transcriptional processes.
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页码:435 / +
页数:26
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共 289 条
[111]  
HORIUCHI J, 1995, MOL CELL BIOL, V15, P1203
[112]   Interaction of human immunodeficiency virus type 1 Tat with the transcriptional coactivators p300 and CREB binding protein [J].
Hotttiger, MO ;
Nabel, GJ .
JOURNAL OF VIROLOGY, 1998, 72 (10) :8252-8256
[113]  
Hsieh YJ, 1999, MOL CELL BIOL, V19, P7697
[114]  
Hung HL, 1999, MOL CELL BIOL, V19, P3496
[115]   REGULATION OF THE SPECIFIC DNA-BINDING FUNCTION OF P53 [J].
HUPP, TR ;
MEEK, DW ;
MIDGLEY, CA ;
LANE, DP .
CELL, 1992, 71 (05) :875-886
[116]   Histone acetyltransferase HBO1 interacts with the ORC1 subunit of the human initiator protein [J].
Iizuka, M ;
Stillman, B .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1999, 274 (33) :23027-23034
[117]  
Ikeda K, 1999, MOL CELL BIOL, V19, P855
[118]   Energy-dependent chromatin remodelers: Complex complexes and their components [J].
Imbalzano, AN .
CRITICAL REVIEWS IN EUKARYOTIC GENE EXPRESSION, 1998, 8 (3-4) :225-255
[119]   FACILITATED BINDING OF TATA-BINDING PROTEIN TO NUCLEOSOMAL DNA [J].
IMBALZANO, AN ;
KWON, H ;
GREEN, MR ;
KINGSTON, RE .
NATURE, 1994, 370 (6489) :481-485
[120]   Acetylation of general transcription factors by histone acetyltransferases [J].
Imhof, A ;
Yang, XJ ;
Ogryzko, VV ;
Nakatani, Y ;
Wolffe, AP ;
Ge, H .
CURRENT BIOLOGY, 1997, 7 (09) :689-692