Graduate Thesis Or Dissertation
 

Active chromatin structure of Saccharomyces cerevisiae : high mobility group proteins, histone modifications and DNase I sensitivity

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  • I examined, in three separate studies, the active chromatin structure of the yeast, Saccharomyces cerevisiae. Yeast contains four proteins having amino acid compositions typical of the high mobility group (HMG) proteins. Three of these are eluted from chromatin by 0.35 M NaCl; one is not, but is eluted by 0.25 N HC1. It follows that HMGs cannot, in general, be defined by extractability criteria. Gel mobilities and amino acid compositions indicate that yeast and animal HMGs have diverged markedly. In a collaborative study the content of the acetylated histone species associated with the highly transcriptionally active chromatin of yeast was found to contain very high levels of the acetylated species for histones H3, H4 and possibly the H2B variants, H2B-1 and H2B-2. Sixty-three percent of the histone H4 species was represented by the di-, tri- and tetra-acetylated forms. These results show yeast chromatin to be among the most highly acetylated of any chromatins reported thus far. DNase I digestion rates were measured for yeast chromatin in the presence and absence of these non-histone chromosomal I.oteins (NHCPs) that are extractable by low salt. This was done with and without butyrate treatment. Removal of the NHCPs from chromatin not treated with butyrate increases the rate of digestion. However, if the chromatin is treated with butyrate, removal of the NHCPs has no discernable effect on the digestion rate.
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