Nucleosome remodeling: one mechanism, many phenomena?
The term 'nucleosome remodeling' subsumes a large number of energy-dependent alterations of canonical nucleosome structure, catalyzed by dedicated ATPases in large multiprotein complexes. The importance of these factors for gene regulation and other processes with chromatin substrate have emerged from genetic studies. Mechanistic analyses of nucleosome remodeling by different enzymes provided a diverse, almost confusing phenomenology of ATP-dependent derangement of nucleosomes in vitro, suggesting that different remodeling machines follow different strategies to disrupt histone-DNA interactions. This review explores the alternative possibility that the rich phenomenology of nucleosome remodeling may be brought about by variations of one basic remodeling reaction.
Längst
Gernot
G
Adolf-Butenandt-Institut, Molekularbiologie, Ludwig-Maximilians-University Munchen, Schillerstrasse 44, D-80336 Munich, Germany.
Becker
Peter B
PB
D000251:Adenosine Triphosphatases / Q000235:genetics / Q000378:metabolism; D042002:Chromatin Assembly and Disassembly / Q000502:physiology*; D004247:DNA / Q000378:metabolism; D004265:DNA Helicases / Q000235:genetics / Q000378:metabolism; D029721:Drosophila Proteins; D024243:HMGB1 Protein / Q000235:genetics / Q000378:metabolism; D009707:Nucleosomes / Q000235:genetics / Q000378:metabolism*; D016601:RNA-Binding Proteins; D017412:Ribonucleoprotein, U1 Small Nuclear / Q000235:genetics / Q000378:metabolism; D014157:Transcription Factors / Q000235:genetics / Q000378:metabolism
D029721:Drosophila Proteins; D024243:HMGB1 Protein; C086468:ISWI protein; D009707:Nucleosomes; D016601:RNA-Binding Proteins; D017412:Ribonucleoprotein, U1 Small Nuclear; D014157:Transcription Factors; C089969:snf protein, Drosophila; D004247:DNA; D000251:Adenosine Triphosphatases; D004265:DNA Helicases