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Cellular protein interactions studied by advanced fluorescence imaging methods
Belejová, Sára ; Heřman, Petr (advisor) ; Krůšek, Jan (referee)
This thesis studies an important tumor suppressor, p53, and its interac�on partner, nucleophosmin (NPM), in living cells. Proteins are studied using fluorescence confocal microscopy techniques such as fluorescence life�me imaging and fluorescence anisotropy measurements. The primary focus of the research is on a specific variant of the p53 protein called p53-L344P, which is generated by a point muta�on from its original form (p53wt). We inves�gate the oligomeriza�on state of p53-L344P in vivo, which appears to be monomeric, confirming the results of in vitro experiments from other studies. Further, we show that p53wt and p53-L344P can form complexes with each other. We compare the interac�on of the NPMmutA protein with p53wt and p53-L344P proteins. Our findings reveal that the L344P mutant is not transferred from the nucleus to the cytoplasm in the presence of NPMmut, as is p53wt. Furthermore, we inves�gate the oligomeriza�on state of p53wt when it is in the cytoplasm and propose avenues for further research into this interac�on.
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