TRICHOSTATIN-A AND TRAPOXIN - NOVEL CHEMICAL PROBES FOR THE ROLE OF HISTONE ACETYLATION IN CHROMATIN STRUCTURE AND FUNCTION

被引：669

作者：

YOSHIDA, M ^{[1
]}

HORINOUCHI, S ^{[1
]}

BEPPU, T ^{[1
]}

机构：

[1] NIHON UNIV, COLL AGR & VET MED, DEPT APPL BIOL SCI, FUJISAWA, KANAGAWA 252, JAPAN

来源：

BIOESSAYS | 1995年 / 17卷 / 05期

关键词：

D O I：

10.1002/bies.950170510

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Reversible acetylation at the epsilon-amino group of lysines located at the conserved domain of core histones is supposed to play an important role in the regulation of chromatin structure and its transcriptional activity. One promising strategy for analyzing the precise function of histone acetylation is to block the activities of acetylating or deacetylating enzymes by specific inhibitors. Recently, two microbial metabolites, trichostatin A and trapoxin, were found to be potent inhibitors of histone deacetylases. Trichostatin A reversibly inhibits the mammalian histone deacetylase, whereas trapoxin causes inhibition through irreversible binding to the enzyme. The histone deacetylase from a trichostatin A-resistant cell line is resistant to trichostatin A, indicating that the enzyme is the primary target. Both of the agents induce a variety of biological responses of cells such as induction of differentiation and cell cycle arrest. Trichostatin A and trapoxin are useful in analyzing the role of histone acetylation in chromatin structure and function as well as in determining the genes whose activities are regulated by histone acetylation.

引用

页码：423 / 430

页数：8

共 74 条

[51] Ikegami S., Et al., Accumulation of multiacetylated forms of histones by trichostatin A and its developmental consequences in early starfish embryos, Roux's Arch. Dev. Biol., 202, pp. 144-151, (1993)
[52] Almouzni G., Khochbin S., Dimitrov S., Wolffe A.P., Histone acetylation influences both gene expression and development of Xenopus laevis, Dev. Biol., 165, pp. 654-669, (1994)
[53] Gorman C.M., Howard B.H., Reeves R., Expression of recombinant plasmids in mammalian cells is enhanced by sodium butyrate, Nucl. Acids Res., 11, pp. 7631-7648, (1983)
[54] Klehr D., Schlake T., Maass K., Bode J., Scaffold‐attached regions (SAR elements) mediate transcriptional effects due to butyrate, Biochemistry, 31, pp. 3222-3229, (1992)
[55] McKnight G.S., Hager L., Palmiter R.D., Butyrate and related inhibitors of histone deacetylation block the induction of egg white genes by steroid hormones, Cell, 22, pp. 469-477, (1980)
[56] Boffa L.C., Walker J., Chen T.A., Sterner R., Mariani M.R., Allfrey V.G., Factors affecting nucleosome structure in transcriptionally active chromatin. Histone acetylation, nascent RNA and inhibitors of RNA synthesis, Eur. J. Biochem., 194, pp. 811-823, (1990)
[57] Schlake T., Klehr-Wirth D., Yoshida M., Beppu T., Bode J., Gene expression within a chromatin domain: the role of core histone hyperacetylation, Biochemistry, 33, pp. 4197-4206, (1994)
[58] Dunaway M., Ostrander E.A., Local domains of supercoiling activate a eukaryotic promoter in vivo, Nature, 361, pp. 746-748, (1993)
[59] Alonso A., Breuer B., Bouterfa H., Doenecke D., Early increase in histone H1° mRNA during differentiation of F9 cells to parietal endoderm, EMBO J., 7, pp. 3003-3008, (1988)
[60] Rousseau D., Khochbin S., Gorka C., Lawrence J.J., Regulation of histone H1° accumulation during induced differentiation of murineerythroleukemia cells, J. Mol. Biol., 217, pp. 85-92, (1991)

← 1 2 3 4 5 6 7 8 →