Functional interaction between GCN5 and polyamines: a new role for core histone acetylation
Authors
Pollard, Kerri JeanneSamuels, Michael L.
Crowley, Kimberly A.
Hansen, Jeffrey C.
Peterson, Craig L.
UMass Chan Affiliations
Department of Biochemistry and Molecular BiologyProgram in Molecular Medicine
Graduate School of Biomedical Sciences
Graduate School of Biomedical Sciences
Document Type
Journal ArticlePublication Date
1999-10-16Keywords
Acetylation; *DNA-Binding Proteins; Fungal Proteins; Histone Acetyltransferases; Histone Deacetylases; Histones; Mutation; Nucleosomes; Polyamines; Protein Kinases; Saccharomyces cerevisiae; *Saccharomyces cerevisiae Proteins; Spermidine; Suppression, Genetic; Transcription, GeneticLife Sciences
Medicine and Health Sciences
Metadata
Show full item recordAbstract
Polyamines are organic polycations essential for a wide variety of cellular functions, including nuclear integrity and chromosome condensation. Here we present genetic evidence that depletion of cellular polyamines partially alleviates the defects in HO and SUC2 expression caused by inactivation of the GCN5 histone acetyltransferase. In addition, the combination of polyamine depletion and a sin(-) allele of the histone H4 gene leads to almost complete bypass of the transcriptional requirement for GCN5. In contrast, polyamine depletion does not alter the transcriptional requirements for the SWI/SNF chromatin remodeling complex nor does depletion lead to global defects in transcriptional regulation. In addition to these genetic studies, we show that polyamines facilitate oligomerization of nucleosomal arrays in vitro, and that polyamine-mediated condensation requires intact core histone N-terminal domains and is inhibited by histone hyperacetylation. Our studies suggest that polyamines are repressors of transcription in vivo, and that one role of histone hyperacetylation is to antagonize the ability of polyamines to stabilize highly condensed states of chromosomal fibers.Source
EMBO J. 1999 Oct 15;18(20):5622-33. Link to article on publisher's siteDOI
10.1093/emboj/18.20.5622Permanent Link to this Item
http://hdl.handle.net/20.500.14038/34349PubMed ID
10523306Related Resources
Link to article in PubMedae974a485f413a2113503eed53cd6c53
10.1093/emboj/18.20.5622