Graduate Thesis Or Dissertation
 

An electrophoretic investigation of nucleoprotein organization in yeast chromatin

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  • I have investigated nucleoprotein organization in chromatin of the yeast, Saccharomyces cerevisiae. My approach has been to prepare insoluble, minimally per turbed chromatin from a mitochondrial DNA-free strain of yeast, using a number of new techniques, and then digest this substrate with micrococcal nuclease. The soluble products are electrophoresed on a newly devised high resolution native nucleoprotein gel; DNA and protein constituents of the resolved complexes are analyzed by means of second dimension electrophoresis. I find that yeast nucleoproteins resolve into two bands for each DNA size class, lack a chromatosome, display a distinctive non-random pattern of nuclease excision for dinucleosomes and larger species, and have a markedly reduced complement of mononucieosomes when prepared in this manner. A single non-core protein of about 32,000 daltons appears to be bound to oligonucleosomes, but in modest amount, and primarily on the trinucleosome. A very prominent 40 kilodalton protein is selectively released by RNase, but is not associated with oligonucleosomes during native electrophoresis. These findings are discussed, with emphasis on nucleosome-nucleosome interactions and mononucleosome stability.
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file details SzentGyorgyiChristopherS1983.pdf 2017-08-07 Öffentlich Herunterladen