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The role of c14orf2 protein in structure and function of mammalian ATP synthase
Ho, Dieu Hien ; Pecina, Petr (advisor) ; Panicucci Zíková, Alena (referee)
The F1Fo-ATP synthase (EC 3.6.3.14) is a key enzyme of the mitochondrial oxidative phosphorylation system (OXPHOS) - using the proton gradient generated by the respiratory chain it synthetizes approximately 90 % of cellular ATP. The subunit arrangement of its Fo domain has not been yet described in detail. At present, the research on ATP synthase research is focused mostly on revealing the structure of the proton channel a so that it is possible to precisely define the molecular mechanism of the ATP synthase rotation generation. The role of the supernumery subunits of Fo domain represents another unresolved issue. These proteins specific for eukaryotic ATP synthases are not essential for synthetic activity, instead they are putatively involved in assembly or stabilization of the enzyme complex. One of such subunits is the nuclear encoded MLQ protein (or also 6.8 kDa proteolipid or MP68), which is conserved only in vertebrates. The aim of this diploma thesis was to reveal the role of this subunit in the structure, assembly and function of the F1Fo-ATP synthase. For these purposes, cellular model of the HEK293 line with the deficiency of the MLQ protein was established employing the CRISPR/Cas9 method with paired nickases (the knock-out MLQ, MLQ KO) as part of the thesis. Three chosen MLQ KO lines...
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New components and functions of mitochondrial ATP synthase.
Ho, Dieu Hien ; Pecina, Petr (advisor) ; Kalous, Martin (referee)
The system of oxidative phosphorylation, or respiratory chain in mitochondria gives the eukaryotic cell total majority of the energy it receives and uses in the form of ATP. F1Fo-ATP synthase, powered by the proton-motive force is directly responsible for the ATP synthesis. Diseases connected to the ATP synthesis can have even lethal consequences. There is therefore no doubt about the need for a detailed analysis of the structure of this enzyme. What is left is to reveal the structure of the transmembrane domains, which are not involved in the synthesis itself, but they can for example work as stabilisers or assembly factors. Outside the synthesis activity the dimers of F1Fo-ATP synthase are apparently taking part in the formation of the cristae of the inner membrane of a mitochondrion. Recently, the role of the enzyme is also considered in the creation of the mitochondrial permeability transition pore.
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The role of c14orf2 protein in structure and function of mammalian ATP synthase
Ho, Dieu Hien ; Pecina, Petr (advisor) ; Panicucci Zíková, Alena (referee)
The F1Fo-ATP synthase (EC 3.6.3.14) is a key enzyme of the mitochondrial oxidative phosphorylation system (OXPHOS) - using the proton gradient generated by the respiratory chain it synthetizes approximately 90 % of cellular ATP. The subunit arrangement of its Fo domain has not been yet described in detail. At present, the research on ATP synthase research is focused mostly on revealing the structure of the proton channel a so that it is possible to precisely define the molecular mechanism of the ATP synthase rotation generation. The role of the supernumery subunits of Fo domain represents another unresolved issue. These proteins specific for eukaryotic ATP synthases are not essential for synthetic activity, instead they are putatively involved in assembly or stabilization of the enzyme complex. One of such subunits is the nuclear encoded MLQ protein (or also 6.8 kDa proteolipid or MP68), which is conserved only in vertebrates. The aim of this diploma thesis was to reveal the role of this subunit in the structure, assembly and function of the F1Fo-ATP synthase. For these purposes, cellular model of the HEK293 line with the deficiency of the MLQ protein was established employing the CRISPR/Cas9 method with paired nickases (the knock-out MLQ, MLQ KO) as part of the thesis. Three chosen MLQ KO lines...
|
|
|
New components and functions of mitochondrial ATP synthase.
Ho, Dieu Hien ; Pecina, Petr (advisor) ; Kalous, Martin (referee)
The system of oxidative phosphorylation, or respiratory chain in mitochondria gives the eukaryotic cell total majority of the energy it receives and uses in the form of ATP. F1Fo-ATP synthase, powered by the proton-motive force is directly responsible for the ATP synthesis. Diseases connected to the ATP synthesis can have even lethal consequences. There is therefore no doubt about the need for a detailed analysis of the structure of this enzyme. What is left is to reveal the structure of the transmembrane domains, which are not involved in the synthesis itself, but they can for example work as stabilisers or assembly factors. Outside the synthesis activity the dimers of F1Fo-ATP synthase are apparently taking part in the formation of the cristae of the inner membrane of a mitochondrion. Recently, the role of the enzyme is also considered in the creation of the mitochondrial permeability transition pore.
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