The phosphorylation state of Saccharomyces cerevisiae linker histone Hho 1p during entry and exit of stationary phase

Our group has recently found that the linker histone Hh01 p of Saccharomyces cerevisiae exhibited a significant increase in binding to chromatin during stationary phase. Because of the role of H1 in gene expression and chromatin compaction, it is essential to understand the mechanism behind this change in binding behaviour for a complete mechanistic description of gene regulation. We postulated that the phosphorylation of serine or threonine residues decrease the affinity of H1 for DNA, resulting in the dissociation of H1 from chromatin in exponential phase. We investigated this possible change in the phosphorylation state of Hh01 p in yeast cells in exponential phase and in stationary phase by immunoprecipitation of Hh01 p, followed by western analysis using antiphosphoserine and anti-phosphothreonine antibodies.

Grantor dc:publisher.institution

Department of Molecular and Cell Biology

Year dc:date.issued

2005

Author dc:creator

• Somers, Sachin J

Advisor dc:contributor.advisor

• Patterton, Hugh

Language dc:language.iso

eng

Handle dc:identifier.uri

http://hdl.handle.net/11427/4335

OAI identifier oai:identifier

oai:open.uct.ac.za:11427/4335