Two functionally distinct forms of the RSC nucleosome-remodeling complex, containing essential AT hook, BAH, and bromodomains Journal Article


Authors: Cairns, B. R.; Schlichter, A.; Erdjument-Bromage, H.; Tempst, P.; Kornberg, R. D.; Winston, F.
Article Title: Two functionally distinct forms of the RSC nucleosome-remodeling complex, containing essential AT hook, BAH, and bromodomains
Abstract: RSC is an essential 15 protein nucleosome-remodeling complex from S. cerevisiae. We have identified two closely related RSC members, Rsc1 and Rsc2. Biochemical analysis revealed Rsc1 and Rsc2 in distinct complexes, defining two forms of RSC. Genetic analysis has shown that Rsc1 and Rsc2 possess shared and unique functions. Rsc1 and Rsc2 each contain two bromodomains, a bromo-adjacent homology (BAH) domain, and an AT hook. One of the bromodomains, the BAH domain, and the AT hook are each essential for Rsc1 and Rsc2 functions, although they are not required for assembly into RSC complexes. Therefore, these domains are required for RSC function. Additional genetic analysis provides further evidence that RSC function is related to transcriptional control.
Keywords: gene mutation; human cell; gene deletion; dna-binding proteins; genetic analysis; phenotype; protein binding; transcription, genetic; transcription factors; nuclear proteins; transcription regulation; amino acid sequence; molecular sequence data; sequence homology, amino acid; recombinant fusion proteins; saccharomyces cerevisiae; sequence alignment; temperature; saccharomyces cerevisiae proteins; sequence homology; dna binding; amino acid motifs; sequence analysis, protein; genes, lethal; nucleosomes; fungal proteins; precipitin tests; human; article
Journal Title: Molecular Cell
Volume: 4
Issue: 5
ISSN: 1097-2765
Publisher: Cell Press  
Date Published: 1999-11-01
Start Page: 715
End Page: 723
Language: English
PUBMED: 10619019
PROVIDER: scopus
DOI: 10.1016/S1097-2765(00)80382-2
DOI/URL:
Notes: Article -- Export Date: 16 August 2016 -- Source: Scopus
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  1. Paul J Tempst
    324 Tempst