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Meiotic recombination in S. cerevisiae is initiated by double-strand breaks (DSBs). In certain mutants, breaks accumulate with a covalently attached protein, suggesting that cleavage is catalyzed by the DSB-associated protein via a topoisomerase-like transesterase mechanism. We have purified these protein-DNA complexes and identified the protein as Spo11,(More)
Chromosome behavior in meiosis is well characterized from cytological and genetic descriptions but little is known of the underlying molecular mechanisms, largely because no one experimental system has been developed to support an integrated application of modern cytological, genetic, and molecular biological methods. To combine efficient analyses of(More)
Amplification of the 8p11-12 region has been found in about 15% of human breast cancers and is associated with poor prognosis. Earlier, we used genomic analysis of copy number and gene expression to perform a detailed analysis of the 8p11-12 amplicon to identify candidate oncogenes in breast cancer. We identified 21 candidate genes and provided evidence(More)
Biclustering algorithms have been successfully used to find subsets of co-expressed genes under subsets of conditions. In some cases, microarray experiments are performed to compare the biological activities of the genes between two classes of cells, such as normal and cancer cells. In this paper, we propose <i>DiBiCLUS</i>, a novel <b>Di</b>fferential(More)
Activated oncogenes are the dominant drivers of malignant progression in human cancer, yet little is known about how the transformation from proto-oncogene to activated oncogene drives the expression of transformed phenotypes. An isogenic model of HER-2-mediated transformation of human mammary epithelial cells was used along with HER-2-amplified human(More)
Here we demonstrate that the Saccharomyces cerevisiae DNA ligase activity, which we previously designated DNA ligase II, is encoded by the genomic DNA sequence YOR005c. Based on its homology with mammalian LIG4, this yeast gene has been named DNL4 and the enzyme activity renamed Dnl4. In agreement with others, we find that DNL4 is not required for(More)
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