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National Repository of Grey Literature 3 records found  Search took 0.01 seconds. 
Vlastnosti DNA vazebných mutant proteinů CSL
 Teska, Mikoláš ; Folk, Petr (advisor) ; Šťovíček, Vratislav (referee)
Notch pathway plays a critical role during the development and life of metazoan organisms. CSL proteins are the component of the Notch pathway that mediates the regulation of target genes. The discovery of CSL-like proteins in yeast raised the question of their function in unicellular organisms which did not utilize the canonical Notch pathway. CSL-homologues in yeast are conserved in parts that are important for DNA binding and for fission yeast proteins it was shown that they bind to CSL recognition elements in vitro. In fission yeast, CSL paralogues Cbf11 and Cbf12 play antagonistic roles in cell adhesion and the coordination of cell and nuclear division. Yeast CSL proteins have long and intrinsically unstructured N- terminal domains compared to metazoan CSL proteins. In this study, we investigated the functional significance of these extended N-termini of CSL proteins by their complete removal. For newly constructed truncated variants of proteins Cbf11 and Cbf12 in Schizosaccharomyces pombe we observed the lack of ability to bind CSL recognition RBP probe. The removal of N-terminal parts of CSL proteins in fission yeast led to the change in their cellular localization. Once strongly preferred nuclear localization changed by the removal of N-terminal domains to cytoplasmic localization with a...
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Vlastnosti DNA vazebných mutant proteinů CSL
 Teska, Mikoláš ; Folk, Petr (advisor) ; Šťovíček, Vratislav (referee)
Notch pathway plays a critical role during the development and life of metazoan organisms. CSL proteins are the component of the Notch pathway that mediates the regulation of target genes. The discovery of CSL-like proteins in yeast raised the question of their function in unicellular organisms which did not utilize the canonical Notch pathway. CSL-homologues in yeast are conserved in parts that are important for DNA binding and for fission yeast proteins it was shown that they bind to CSL recognition elements in vitro. In fission yeast, CSL paralogues Cbf11 and Cbf12 play antagonistic roles in cell adhesion and the coordination of cell and nuclear division. Yeast CSL proteins have long and intrinsically unstructured N- terminal domains compared to metazoan CSL proteins. In this study, we investigated the functional significance of these extended N-termini of CSL proteins by their complete removal. For newly constructed truncated variants of proteins Cbf11 and Cbf12 in Schizosaccharomyces pombe we observed the lack of ability to bind CSL recognition RBP probe. The removal of N-terminal parts of CSL proteins in fission yeast led to the change in their cellular localization. Once strongly preferred nuclear localization changed by the removal of N-terminal domains to cytoplasmic localization with a...
Detailed record
Notch-independent functions of CSL transcription factors
 Teska, Mikoláš ; Folk, Petr (advisor) ; Převorovský, Martin (referee) ; Kuthan, Martin (referee)
Notch pathway plays a critical role during development and life of Metazoan organisms. CBF1 is a component of the Notch pathway that mediates the regulation of target genes. The discovery of CBF1-like proteins in yeast raised the question of their function in unicellular organisms - before the origin of canonical Notch pathway. CBF1-homologs in yeast are conserved in parts that are important for DNA binding and bind to CBF1-binding elements in vitro. CBF1 and related transcription factors in Metazoa (CSL) interact with many proteins in Notch-dependent as well as Notch-independent complexes. The Notch receptor has likewise some CSL-independent functions. This assay reports about interacting partners of CSL in Metazoa along with homologous proteins in yeast with the aim to highlight potential interactions of CBF1-homologs in evolutionary ancestral context.
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