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Developmental specifics of individuals with Angelman and Prader - Willi syndrome as the basis for special educator's work The thesis deals in a complex way with the issue of two rare syndromes - Angelman and Prader- Willi syndrome. It describes the manifestations and genetic background, outlines the options for special education and rehabilitation interventions as well as selected medical and regime measures. The thesis informs about the category of rare diseases and also mentions the strategies for approach to these diseases used in the Czech Republic. It also comprises a list of organizations in the Czech Republic that deal with the Angelman and Prader - Willi syndrome and which associate parents and others interested in this topic. The end, the thesis comprises casuistry of two individuals, characteristic syndrome bearers, and conclusions of a questionnaire survey among parents. Surveys through questionnaires illustrate the specific characteristics of inidividuals that have been used to define areas of support. The goal of the thesis was to describe the possibilities for pedagogic and other interdisciplinary interventions, map the situation in the Czech Republic, and to provide more information about this issue to anyone interested.

Ddi1-like protein family has been recently raised into the spotlight by the scientific community due to its important roles in cellular homeostasis maintenance. It represents a specific group among shuttling proteins of the ubiquitin-proteasome system. When compared to other shuttles, Ddi1-like protein family members harbor a unique retroviral-protease like domain besides the conventional ubiquitin-like (UBL) domain and domains interacting with ubiquitin. In addition, a helical domain of Ddi (HDD) has been recently found in most of the orthologs. In this thesis, I focus on characterization of several members of Ddi1-like protein family, both on molecular level using NMR and in model mouse strains via a variety of biological methods. Solution structure of the UBL domain of Ddi1p of S. cerevisiae was solved and its characteristics were compared to those of the UBL domain of its human ortholog. Furthermore, we show that human DDI2 specifically binds to ubiquitin with its terminal domains, both the UBL and the UIM; however, with very low affinity in contrast to binding properties of its yeast counterpart. Our study also show that hDDI2 does not form a head-to-tail homodimer. Based on our structural studies, we hypothesize that human DDI2 might have evolved a different function compared to its yeast...