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Original title:
The Diverged Trypanosome MICOS Complex as a Hub for Mitochondrial Cristae Shaping and Protein Import
Authors: HELLER, Jiří
Document type: Rigorous theses
Year: 2019
Language: eng
Abstract: This work deals with MICOS, which stands for mitochondrial contact site and cristae organization system. Until now this multiprotein complex has been analyzed experimentally only in yeast and mammals, who belong to the supergroup Opisthokonta. Our study was done on the parasitic protist T. brucei, a member of the another supergroup called Excavata, which is very diverged from opisthokonts.Thus, it is the very first study done outside of Opisthokonta. This could be very useful in the future for a comparative analysis approach. Our results show that the MICOS complex in T. brucei is composed of 9 subunits, most of which are essential for normal growth. It is required for the maintenance of discoidal cristae that typify excavates such as kinetoplastids and euglenids and mediating the mitochondrial outer and inner membranes contacts. In addition, we discovered that the mitochondrial contact site and cristae organization system may participate in the intermembrane space protein import and help in the oxydative phosphorylation complex formation. It seems that this interesting complex is involved in even more cellular processes.
Keywords: cristae; MICOS; mitochondria; protein; trypanosoma
Citation: HELLER, Jiří. The Diverged Trypanosome MICOS Complex as a Hub for Mitochondrial Cristae Shaping and Protein Import. České Budějovice, 2019. rigorózní práce (RNDr.). JIHOČESKÁ UNIVERZITA V ČESKÝCH BUDĚJOVICÍCH. Přírodovědecká fakulta
Institution: University of South Bohemia in České Budějovice (web)
Document availability information: Fulltext is available in the Digital Repository of University of South Bohemia.
Original record: http://www.jcu.cz/vskp/56711
Permalink: http://www.nusl.cz/ntk/nusl-393984
The record appears in these collections:
Universities and colleges > Public universities > University of South Bohemia in České Budějovice
Academic theses (ETDs) > Rigorous theses
Authors: HELLER, Jiří
Document type: Rigorous theses
Year: 2019
Language: eng
Abstract: This work deals with MICOS, which stands for mitochondrial contact site and cristae organization system. Until now this multiprotein complex has been analyzed experimentally only in yeast and mammals, who belong to the supergroup Opisthokonta. Our study was done on the parasitic protist T. brucei, a member of the another supergroup called Excavata, which is very diverged from opisthokonts.Thus, it is the very first study done outside of Opisthokonta. This could be very useful in the future for a comparative analysis approach. Our results show that the MICOS complex in T. brucei is composed of 9 subunits, most of which are essential for normal growth. It is required for the maintenance of discoidal cristae that typify excavates such as kinetoplastids and euglenids and mediating the mitochondrial outer and inner membranes contacts. In addition, we discovered that the mitochondrial contact site and cristae organization system may participate in the intermembrane space protein import and help in the oxydative phosphorylation complex formation. It seems that this interesting complex is involved in even more cellular processes.
Keywords: cristae; MICOS; mitochondria; protein; trypanosoma
Citation: HELLER, Jiří. The Diverged Trypanosome MICOS Complex as a Hub for Mitochondrial Cristae Shaping and Protein Import. České Budějovice, 2019. rigorózní práce (RNDr.). JIHOČESKÁ UNIVERZITA V ČESKÝCH BUDĚJOVICÍCH. Přírodovědecká fakulta
Institution: University of South Bohemia in České Budějovice (web)
Document availability information: Fulltext is available in the Digital Repository of University of South Bohemia.
Original record: http://www.jcu.cz/vskp/56711
Permalink: http://www.nusl.cz/ntk/nusl-393984
The record appears in these collections:
Universities and colleges > Public universities > University of South Bohemia in České Budějovice
Academic theses (ETDs) > Rigorous theses
Record created 2019-03-28, last modified 2023-03-12