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Investigation of newly discovered protein GL50803_16424 in Giardia intestinalis.
Pelc, Josef ; Doležal, Pavel (advisor) ; Pyrih, Jan (referee)
The anaerobic unicellular eukaryotic organism Giardia intestinalis is a worldwide parasite. Giardiasis, the intestinal disease caused by Giardia, is one of the most common parasitic disease in the developed part of the world, that causes health problems not only to humans but also to animals. This organism is also interesting for its many unique cellular features. One of them is the presence of mitosomes - the organelles derived from mitochondria. Analogously to mitochondria, mitosome is limited by two membranes and shares the mode of the protein transport. However, mitosome does not have its own genome and as far as we know, there is only one pathway of the iron-sulfur cluster biosynthesis in this organelle. Using the in vivo enzymatic tagging technique, several novel mitosomal proteins were identified, including GL50803_16424. The protein GL50803_16424 attracted our attention by interacting with components of all mitosomal subcompartments: the outer membrane, the membrane and the matrix. In addition, the expression of HA-tagged GL50803_16424 resulted in the formation of peculiar structures near the mitosomes never seen before in G. intestinalis. Bioinformatic approaches revealed that the GL50803_16424 has domain similar to the myelodysplasia- myeloid leukemia factor 1-interacting protein. Our...
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Export of biomolecules from mitochondria
Pelc, Josef ; Doležal, Pavel (advisor) ; Kovalčíková, Jana (referee)
Mitochondrion is cellular organelle evolved from the endosymbiotic bacteria. Because of its bacterial origin mitochondrion has a number of unique properties and metabolic pathways. Mitochondria or its reduced forms are present in all eukaryotic organisms except a single exception. During the course of evolution most of mitochondrial DNA was transferred to the nucleus. Despite this, mitochondria still encode several proteins that are part of the electron transport chain and the ATP synthase. These proteins are transported from the mitochondrial matrix into the inner mitochondrial membrane. Misfolded proteins of the inner membrane are degraded by mitochondrial proteases, which leads to the release of generated peptides. Fe-S clusters are assembled in the mitochondrial matrix. Still unknown molecule, which is product of ISC pathway is transported into cytosol and participates in the assembly of cytosolic and nuclear iron-sulfur proteins. Other transport pathway ensures the exchange of lipids between the endoplasmic reticulum and mitochondria. Both mitochondrial membranes have different lipid composition. To maintain their properties specific lipid transport is required between the two mitochondrial membranes. This transport pathway is also used for the lipid synthesis in the inner mitochondrial membrane.
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