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National Repository of Grey Literature 2 records found  Search took 0.00 seconds. 
Cellular factors influencing the antibiotic resistance by ABC-F proteins
 Kýr, Jan ; Balíková Novotná, Gabriela (advisor) ; Dolejšová, Tereza (referee)
Antibiotic resistance is one of the main problems modern medicine has to face. In order to control it, it is important first to understand the mechanisms by which resistant pathogens bypass antibiotic treatment. One of the important protein families conferring resistance to 50S binding antibiotics is the ARE ABC-F protein family. A member of this protein family is the MsrA protein, which confers resistance to 14- and 15-membered macrolides. Loss-of-function mutations in the non-essential chaperone ClpX were found to a significant ly enhance the action of the MsrA protein. This leads to the significant increase in the resistance conferred by this protein. The exact mechanism by which ClpX affects MsrA function is still unknown. In this the diploma thesis was demonstrated that chaperone protein ClpX affects the resistance to erythromycin conferred by MsrA protein, due to the interaction with an unknown essential protein, which is mediated by a functional N-terminal zinc-binding domain of the chaperone. Furthermore, it was demonstrated in this work that loss of GluTR function influence the MsrA ability to confer resistance. The results of this work will bet he basis for further reasearch, which will lead to a more detailed understanding of the mechanism of resistance conferred by these proteins and...
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The function of ClpX chaperone in bacteria
 Kýr, Jan ; Balíková Novotná, Gabriela (advisor) ; Šiková, Michaela (referee)
Intracellular proteolysis is an essential regulatory process that affects cellular physiology. Since proteolysis destroys proteins irreversibly, this process must be strictly controlled. The AAA+ proteins are the key factors in regulated proteolysis in bacteria. These proteins consist of two functional domains, the AAA+ chaperone domain and the protease domain. One particular group of these AAA+ protein is the Clp protein family. Functional domains of the Clp family are formed by seperate proteins. The hexameric unfoldase ClpX is a member of this protein family. This unfoldase can interact with the highly conserved ClpP protease to form a ClpXP proteolytic complex. This proteolytic complex utilizes the energy of ATP binding and hydrolysis to unfold and translocate the specifically tagged substrate into the ClpP degradation chamber. Substrate recognition is mediated by the binding of ClpX to short unstructured sequences called degradation tags. ClpX recognizes several degradation tags, but the most important one is recognition of the ssrA degradation tag, which is the output of the tmRNA ribosome rescue system. Although ClpX interacts with ClpP, it affects a variety of cellular processes such as the expression of virulence factors or the adaptation to stress factors, ClpX can work independently of...
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