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Mutant p53 protein and its binding and transactivation properties
Vojsovič, Matúš ; Němcová, Andrea (referee) ; Brázda, Václav (advisor)
The "genome guardian" protein p53 plays an important role in cancer growth. P53 mutations occur in more than 50 % of human cancers. Mutated proteins significantly affect the proper functioning of cells. Due to the mutation, proteins can gain, but also lose, some of their functions, which also help them in modulating cell metabolism. Mutant forms of p53 may be involved in indirect binding or direct binding to DNA. They appeared to have a lower binding activity to the DNA than non-mutated p53. The experimental part of the thesis focuses on measuring the binding properties of selected p53 mutants using gel retardation analysis and using an atomic force microscope and monitoring the transactivation potential. The results were compared with the wild-type form of p53. It has been found that binding to the most common types of local DNA structures reduces the binding activity of p53 mutants over the wild-type. P53 mutants has been shown to have a lower intensity of transactivation than the wild-type p53 by studying their transactivation abilities and also they are able to reduce the intensity of transactivation when co-expressed with p53.
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Mutant p53 protein and its binding and transactivation properties
Vojsovič, Matúš ; Němcová, Andrea (referee) ; Brázda, Václav (advisor)
The "genome guardian" protein p53 plays an important role in cancer growth. P53 mutations occur in more than 50 % of human cancers. Mutated proteins significantly affect the proper functioning of cells. Due to the mutation, proteins can gain, but also lose, some of their functions, which also help them in modulating cell metabolism. Mutant forms of p53 may be involved in indirect binding or direct binding to DNA. They appeared to have a lower binding activity to the DNA than non-mutated p53. The experimental part of the thesis focuses on measuring the binding properties of selected p53 mutants using gel retardation analysis and using an atomic force microscope and monitoring the transactivation potential. The results were compared with the wild-type form of p53. It has been found that binding to the most common types of local DNA structures reduces the binding activity of p53 mutants over the wild-type. P53 mutants has been shown to have a lower intensity of transactivation than the wild-type p53 by studying their transactivation abilities and also they are able to reduce the intensity of transactivation when co-expressed with p53.
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