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S. pombe Sin3 homolog Pst3 is Key in Nucleolar Integrity

ABSTRACT: The Sin3/HDAC complex is highly conserved from yeast to humans. Sin3 provides the scaffolding needed to coordinate DNA binding proteins with various chromatin modifying enzymes, most often histone deacetylases, to establish chromatin environments important both for correct gene regulation and genome stability (reviewed in [1]). Three Sin3 homologs are present. Here we explore Pst3, the most ancient of the Sin3 molecules, in Schizosaccharomyces pombe. In contrast to Pst1 [2] and Pst2 [3], Pst3 occupies the entire nuclear space, including the nucleolus. The deletion of pst3+ causes general genome instability including chomosome mis-segregation, gross sporulation defects, rampant anneuploidy, and distended nucleoli. Genome-wide expression analysis indicated a role in both gene repression and gene activation. Interestingly, highly expressed genes encoding ribosomal and nucleolar proteins were positively regulated by Pst3. Genome wide binding analysis for Pst3-GFP indicated that Pst3 is bound both to intergenic and coding regions, and could be correlated with expression data. Proteins previously identified as part of the Clr6/Pst2 complex co-immunopercipitated with Pst3-TAP. Additionally, Snf59, the kinase Ssp1, and the Dead-Box helicase Dbp10 were identified as Pst3 interaction partners. Taken together this data suggests that Pst3 has a direct role in the structure and function of the nucleolus. Keywords: Expression profiling Expression profiling experiments were performed and quantified according to (Xue et al., 2004).

ORGANISM(S): Schizosaccharomyces pombe

SUBMITTER: Julian Walfridsson

PROVIDER: E-GEOD-7133 | biostudies-arrayexpress |

REPOSITORIES: biostudies-arrayexpress

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