title: RSC, an essential, abundant chromatin-remodeling complex.
abstract: A novel 15-subunit complex with the capacity to remodel the structure of chromatin, termed RSC, has been isolated from S. cerevisiae on the basis of homology to the SWI/SNF complex. At least three RSC subunits are related to SWI/SNF polypeptides: Sth1p, Rsc6p, and Rsc8p are significantly similar to Swi2/Snf2p, Swp73p, and Swi3p, respectively, and were identified by mass spectrometric and sequence analysis of peptide fragments. Like SWI/SNF, RSC exhibits a DNA-dependent ATPase activity stimulated by both free and nucleosomal DNA and a capacity to perturb nucleosome structure. RSC is, however, at least 10-fold more abundant than SWI/SNF complex and is essential for mitotic growth. Contrary to a report for SWII/SNF complex, no association of RSC (nor of SWI/SNF complex) with RNA polymerase II holoenzyme was detected.
authors.affiliation: Department of Structural Biology, Stanford University School of Medicine, California 94305, USA.
authors.forename: B R
authors.initials: BR
authors.lastname: Cairns
authors.forename: Y
authors.initials: Y
authors.lastname: Lorch
authors.forename: Y
authors.initials: Y
authors.lastname: Li
authors.forename: M
authors.initials: M
authors.lastname: Zhang
authors.forename: L
authors.initials: L
authors.lastname: Lacomis
authors.forename: H
authors.initials: H
authors.lastname: Erdjument-Bromage
authors.forename: P
authors.initials: P
authors.lastname: Tempst
authors.forename: J
authors.initials: J
authors.lastname: Du
authors.forename: B
authors.initials: B
authors.lastname: Laurent
authors.forename: R D
authors.initials: RD
authors.lastname: Kornberg
mesh_terms: D000123:Acetyltransferases / Q000378:metabolism; D000251:Adenosine Triphosphatases / Q000737:chemistry*; D000255:Adenosine Triphosphate / Q000378:metabolism; D000595:Amino Acid Sequence; D018797:Cell Cycle Proteins; D002843:Chromatin / Q000648:ultrastructure*; D002868:Chromosomal Proteins, Non-Histone / Q000502:physiology*; D004265:DNA Helicases; D004268:DNA-Binding Proteins / Q000502:physiology*; D005656:Fungal Proteins / Q000502:physiology*; D015966:Gene Expression Regulation, Fungal; D005800:Genes, Fungal; D051548:Histone Acetyltransferases; D046911:Macromolecular Substances; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D009687:Nuclear Proteins / Q000502:physiology*; D009707:Nucleosomes / Q000648:ultrastructure*; D017433:Protein Structure, Secondary; D012319:RNA Polymerase II / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000235:genetics*; D029701:Saccharomyces cerevisiae Proteins; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D015534:Trans-Activators; D014157:Transcription Factors / Q000737:chemistry* / Q000502:physiology*
chemical_list: D018797:Cell Cycle Proteins; D002843:Chromatin; D002868:Chromosomal Proteins, Non-Histone; D004268:DNA-Binding Proteins; D005656:Fungal Proteins; D046911:Macromolecular Substances; D009687:Nuclear Proteins; D009707:Nucleosomes; C103337:RSC complex, S cerevisiae; C101683:SNF12 protein, S cerevisiae; C072981:SWI3 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins; D015534:Trans-Activators; D014157:Transcription Factors; D000255:Adenosine Triphosphate; D000123:Acetyltransferases; D051548:Histone Acetyltransferases; D012319:RNA Polymerase II; D000251:Adenosine Triphosphatases; C499333:SNF2 protein, S cerevisiae; C077392:STH1 protein, S cerevisiae; D004265:DNA Helicases