Document Detail

Trichostatin A and trapoxin: novel chemical probes for the role of histone acetylation in chromatin structure and function.
MedLine Citation:
PMID:  7786288     Owner:  NLM     Status:  MEDLINE    
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.
M Yoshida; S Horinouchi; T Beppu
Related Documents :
18614528 - Structural and functional analysis of the human hdac4 catalytic domain reveals a regula...
12540238 - Synthesis, anti-hiv activity, and molecular mechanism of drug resistance of l-2',3'-did...
11931768 - The n-cor-hdac3 nuclear receptor corepressor complex inhibits the jnk pathway through t...
16728978 - Molecular basis for site-specific read-out of histone h3k4me3 by the bptf phd finger of...
12682008 - A redox-sensitive loop regulates plasminogen activator inhibitor type 2 (pai-2) polymer...
24196958 - Glu44 in the amino-terminal α-helix of yeast v-atpase e subunit (vma4p) has a role for...
Publication Detail:
Type:  Journal Article; Review    
Journal Detail:
Title:  BioEssays : news and reviews in molecular, cellular and developmental biology     Volume:  17     ISSN:  0265-9247     ISO Abbreviation:  Bioessays     Publication Date:  1995 May 
Date Detail:
Created Date:  1995-07-17     Completed Date:  1995-07-17     Revised Date:  2005-11-17    
Medline Journal Info:
Nlm Unique ID:  8510851     Medline TA:  Bioessays     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  423-30     Citation Subset:  IM    
Department of Biotechnology, University of Tokyo, Japan.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Anti-Bacterial Agents / metabolism*,  pharmacology
Chromatin / chemistry,  metabolism*
Gene Expression Regulation
Histones / chemistry,  metabolism*
Hydroxamic Acids / metabolism*,  pharmacology
Transcription, Genetic
Reg. No./Substance:
0/Anti-Bacterial Agents; 0/Chromatin; 0/Histones; 0/Hydroxamic Acids; 0/Peptides; 133155-89-2/trapoxin A; 58880-19-6/trichostatin A

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

Previous Document:  Seminal plasmin.
Next Document:  A radical approach to enzyme catalysis.