Metabolomics,Unknown,Transcriptomics,Genomics,Proteomics

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Transcription profiling of S. cerevisiae wild type and spt10 mutant strains


ABSTRACT: Using yeast strains based on the protease-deficient strain BJ5459 (= wild type), the effects of the spt10-null and spt10-C388S mutations on global gene expression were assessed and compared. BJ5459 (wild type) and BJ-SPT10(C388S)-HA cells were grown in synthetic complete medium to A600 = 0.6. RNA was prepared using an RNeasy kit (Qiagen). Biotinylated cRNA was prepared from three independently prepared sample pairs and hybridised to Affymetrix S98 arrays and detected using fluorescently labelled streptavidin. The wild type and the spt10-C388S average signals each represent the average of the signals from three arrays. The P-value is an indicator of the statistical significance of the difference between the average signals for wild type and the C388S mutant. The lower the value, the greater the significance. The gene descriptor is provided by Affymetrix. Experiment Overall Design: Three RNA samples from wild type, spt10-null and spt10-C388S cells were prepared independently on three occasions. These nine RNA samples were used to make cRNA and hybridised separately to Affymetrix S98 arrays at the same time.

ORGANISM(S): Saccharomyces cerevisiae

SUBMITTER: David Johannes Clark 

PROVIDER: E-GEOD-3354 | biostudies-arrayexpress |

REPOSITORIES: biostudies-arrayexpress

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Publications

The DNA-binding domain of the yeast Spt10p activator includes a zinc finger that is homologous to foamy virus integrase.

Mendiratta Geetu G   Eriksson Peter R PR   Shen Chang-Hui CH   Clark David J DJ  

The Journal of biological chemistry 20060116 11


The yeast SPT10 gene encodes a putative histone acetyltransferase that binds specifically to pairs of upstream activating sequence (UAS) elements found only in the histone gene promoters. Here, we demonstrate that the DNA-binding domain of Spt10p is located between residues 283 and 396 and includes a His(2)-Cys(2) zinc finger. The binding of Spt10p to the histone UAS is zinc-dependent and is disabled by a zinc finger mutation (C388S). The isolated DNA-binding domain binds to single histone UAS e  ...[more]

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