SWRred not shaken; mixing the histones.
The recently isolated SWR1 complex catalyzes an ATP-dependent histone exchange with specificity for the histone variant H2A.Z. This provides a new theme in chromatin remodeling mechanisms and an explanation of how histone variants are incorporated into the nucleosome outside of S phase. In connection with the isolation of histone variant specific chaperone complexes, we are beginning to see the mechanisms that mix the histone octamer with intriguing implications for epigenetic inheritance.
Korber
Philipp
P
Adolf-Butenandt-Institut, Molekularbiologie, Universität München, Schillerstr. 44, 80336 München, Germany.
Hörz
Wolfram
W
D000251:Adenosine Triphosphatases / Q000235:genetics*; D002453:Cell Cycle / Q000235:genetics; D002843:Chromatin / Q000235:genetics*; D042002:Chromatin Assembly and Disassembly / Q000235:genetics*; D006657:Histones / Q000235:genetics*; D046911:Macromolecular Substances; D018832:Molecular Chaperones / Q000235:genetics; D009707:Nucleosomes / Q000235:genetics*; D029701:Saccharomyces cerevisiae Proteins / Q000235:genetics*
D002843:Chromatin; D006657:Histones; D046911:Macromolecular Substances; D018832:Molecular Chaperones; D009707:Nucleosomes; D029701:Saccharomyces cerevisiae Proteins; D000251:Adenosine Triphosphatases; C481261:Swr1 protein, S cerevisiae