Reference: Sikder D, et al. (2006) Widespread, but non-identical, association of proteasomal 19 and 20 S proteins with yeast chromatin. J Biol Chem 281(37):27346-55

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Abstract

It has recently become clear that various aspects of nucleic acid metabolism and the ubiquitin-proteasome pathway intersect in several direct and important ways. To begin to assess the scope of some of these activities is the yeast Saccharomyces cerevisiae, we have assessed the physical and functional association of proteasomal proteins from both the 20S core and 19S regulatory particles with approximately 6400 yeast genes. Genome-wide chromatin immunoprecipitation analyses reveal that proteasome substituents are associated with the majority of yeast genes. Many of these associations correlate strongly with expression levels and the presence of RNA polymerase II. While the data support the presence of the intact 26S proteasome on most genes, several hundred yeast genes cross-link to either the 20S or 19S complex, but not both, consistent with some degree of independent function for the proteasomal sub-complexes.

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Journal Article
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Sikder D, Johnston SA, Kodadek T
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