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PMID: 8608939 Published · ppublish English Journal Article Review

Repression and activation by multiprotein complexes that alter chromatin structure.

Genes & development ·Vol. 10 ·No. 8 ·1996-04-15 ·Pages 905-20

Kingston RE, Bunker CA, Imbalzano AN

Abstract

Recent studies have provided strong evidence that macromolecular complexes are used in the cell to remodel chromatin structure during activation and to create an inaccessible structure during repression, Although there is not yet any rigorous demonstration that modification of chromatin structure plays a direct, causal role in either activation or repression, there is sufficient smoke to indicate the presence of a blazing inferno nearby. It is clear that complexes that remodel chromatin are tractable in vitro; hopefully this will allow the establishment of systems that provide a direct analysis of the role that remodeling might play in activation. These studies indicate that establishment of functional systems to corroborate the elegant genetic studies on repression might also be tractable. As the mechanistic effects of these complexes are sorted out, it will become important to understand how the complexes are regulated. In many of the instances discussed above, the genes whose products make up these complexes were identified in genetic screens for effects on developmental processes. This implies a regulation of the activity of these complexes in response to developmental cues and further implies that the work to fully understand these complexes will occupy a generation of scientists.

MeSH Terms
Adenosine Triphosphate/physiology Animals Chromatin/ultrastructure Chromosomal Proteins, Non-Histone DNA-Binding Proteins/physiology Drosophila Proteins Drosophila melanogaster/genetics Fungal Proteins/physiology Gene Expression Regulation Macromolecular Substances Nuclear Proteins Nucleosomes/physiology,ultrastructure RNA-Binding Proteins Repressor Proteins/physiology Ribonucleoprotein, U1 Small Nuclear/genetics Saccharomyces cerevisiae/genetics Saccharomyces cerevisiae Proteins Telomere Transcription Factors/physiology Transcription, Genetic
Chemicals
CYC8 protein, S cerevisiae Chromatin Chromosomal Proteins, Non-Histone DNA-Binding Proteins Drosophila Proteins Fungal Proteins Macromolecular Substances Nuclear Proteins Nucleosomes RNA-Binding Proteins Repressor Proteins Ribonucleoprotein, U1 Small Nuclear SWI1 protein, S cerevisiae Saccharomyces cerevisiae Proteins Transcription Factors snf protein, Drosophila Adenosine Triphosphate
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Kingston R E
Department of Molecular Biology, Massachusetts General Hospital, Boston, Massachusetts, 02114, USA.
Bunker C A
Imbalzano A N
Article Info
Journal
Genes & development
Abbr.
Genes Dev
ISSN
0890-9369
Published
1996-04-15
Pages
905-20
Language
English
Region
United States
NLM ID
8711660
Subset
IM
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