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Microarray analysis comparing yeast Eco1 mutant W216G to mutants of FOB1 and RAD61


ABSTRACT: Eco1 is an acetyltransferase subunit of the cohesin complex and acts during DNA replication to establish cohesion between sister chromatids. However, cohesin has additional functions in gene expression, DNA damage repair, and higher-order organization of chromosomes. The eco1 mutant W216G disrupts acetyltansferase activity, and causes genome-wide transcriptional defects which can be suppressed by deletion of FOB1, a gene also involved in DNA replication. This experiment investigates gene expression differences between the eco1-W216G mutant, and mutants in FOB1, and RAD61 a gene involved in inhibition of cohesion establishment but mutation of which is able to suppress temperature sensitivity of the eco1-W216G mutant. Wt and mutant strains of yeast were grown to mid log phase in liquid culture in triplicate and harvested for comparison on Affymetrix microarrays. The following strains were compared: 1) eco1-W216G, 2) eco1-W216G fob1Δ, 3) eco1-W216G rad61Δ, 4) fob1Δ, 5) rad61Δ, and 6) WT.

ORGANISM(S): Saccharomyces cerevisiae

SUBMITTER: Chris Seidel 

PROVIDER: E-GEOD-54741 | biostudies-arrayexpress |

REPOSITORIES: biostudies-arrayexpress

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Publications

The cohesin acetyltransferase Eco1 coordinates rDNA replication and transcription.

Lu Shuai S   Lee Kenneth K KK   Harris Bethany B   Xiong Bo B   Bose Tania T   Saraf Anita A   Hattem Gaye G   Florens Laurence L   Seidel Chris C   Gerton Jennifer L JL  

EMBO reports 20140314 5


Eco1 is the acetyltransferase that establishes sister-chromatid cohesion during DNA replication. A budding yeast strain with an eco1 mutation that genocopies Roberts syndrome has reduced ribosomal DNA (rDNA) transcription and a transcriptional signature of starvation. We show that deleting FOB1--a gene that encodes a replication fork-blocking protein specific for the rDNA region--rescues rRNA production and partially rescues transcription genome-wide. Further studies show that deletion of FOB1 c  ...[more]

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