GSBS Student Publications

Title

Functional interaction between GCN5 and polyamines: a new role for core histone acetylation

UMMS Affiliation

Graduate School of Biomedical Sciences; Graduate School of Biomedical Sciences; Program in Molecular Medicine; Department of Biochemistry and Molecular Biology

Date

10-16-1999

Document Type

Article

Medical Subject Headings

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, Genetic

Disciplines

Life Sciences | Medicine and Health Sciences

Abstract

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.

Rights and Permissions

Citation: EMBO J. 1999 Oct 15;18(20):5622-33. Link to article on publisher's site

Related Resources

Link to article in PubMed

Journal Title

The EMBO journal

PubMed ID

10523306