Structural and Functional Characterization of Clp Chaperones and Proteases in the Human Malaria Parasite Plasmodium falciparum
The Clp chaperones and proteases play a pivotal role in maintaining cellular homeostasis. They are highly conserved across prokaryotes and can also be found in the mitochondria of eukaryotes and chloroplast of plants. For my thesis, I provide an analysis of the Clp chaperones and protease in the hum...
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ndltd-LACETR-oai-collectionscanada.gc.ca-OTU.1807-334932013-11-02T03:43:50ZStructural and Functional Characterization of Clp Chaperones and Proteases in the Human Malaria Parasite Plasmodium falciparumPow, AndreClpproteasechaperoneapicoplastPlasmodium falciparumPfClpATPasesPfClpPPfClpRThe Clp chaperones and proteases play a pivotal role in maintaining cellular homeostasis. They are highly conserved across prokaryotes and can also be found in the mitochondria of eukaryotes and chloroplast of plants. For my thesis, I provide an analysis of the Clp chaperones and protease in the human malaria parasite Plasmodium falciparum. The parasite contains four Clp ATPases, which I term PfClpB1, PfClpB2, PfClpC, and PfClpM. One PfClpP, the proteolytic protomer, and one PfClpR, an inactive isoform, were also identified. All proteins, with the exception of PfClpB2, were found to be localized to the apicoplast, a non-photosynthetic relic plastid in P. falciparum. Both PfClpP and PfClpR form mostly homoheptameric rings as observed by various techniques. Through X-ray crystallography, PfClpP assumed a compacted tetradecamer structure similar to that observed for other ClpPs. My data suggest the presence of a ClpCRP complex in the apicoplast of P. falciparum.Houry, Walid A.2012-112012-11-26T16:47:28ZNO_RESTRICTION2012-11-26T16:47:28Z2012-11-26Thesishttp://hdl.handle.net/1807/33493en_ca |
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Clp protease chaperone apicoplast Plasmodium falciparum PfClp ATPases PfClpP PfClpR |
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Clp protease chaperone apicoplast Plasmodium falciparum PfClp ATPases PfClpP PfClpR Pow, Andre Structural and Functional Characterization of Clp Chaperones and Proteases in the Human Malaria Parasite Plasmodium falciparum |
description |
The Clp chaperones and proteases play a pivotal role in maintaining cellular homeostasis. They are highly conserved across prokaryotes and can also be found in the mitochondria of eukaryotes and chloroplast of plants. For my thesis, I provide an analysis of the Clp chaperones and protease in the human malaria parasite Plasmodium falciparum. The parasite contains four Clp ATPases, which I term PfClpB1, PfClpB2, PfClpC, and PfClpM. One PfClpP, the proteolytic protomer, and one PfClpR, an inactive isoform, were also identified. All proteins, with the exception of PfClpB2, were found to be localized to the apicoplast, a non-photosynthetic relic plastid in P. falciparum. Both PfClpP and PfClpR form mostly homoheptameric rings as observed by various techniques. Through X-ray crystallography, PfClpP assumed a compacted tetradecamer structure similar to that observed for other ClpPs. My data suggest the presence of a ClpCRP complex in the apicoplast of P. falciparum. |
author2 |
Houry, Walid A. |
author_facet |
Houry, Walid A. Pow, Andre |
author |
Pow, Andre |
author_sort |
Pow, Andre |
title |
Structural and Functional Characterization of Clp Chaperones and Proteases in the Human Malaria Parasite Plasmodium falciparum |
title_short |
Structural and Functional Characterization of Clp Chaperones and Proteases in the Human Malaria Parasite Plasmodium falciparum |
title_full |
Structural and Functional Characterization of Clp Chaperones and Proteases in the Human Malaria Parasite Plasmodium falciparum |
title_fullStr |
Structural and Functional Characterization of Clp Chaperones and Proteases in the Human Malaria Parasite Plasmodium falciparum |
title_full_unstemmed |
Structural and Functional Characterization of Clp Chaperones and Proteases in the Human Malaria Parasite Plasmodium falciparum |
title_sort |
structural and functional characterization of clp chaperones and proteases in the human malaria parasite plasmodium falciparum |
publishDate |
2012 |
url |
http://hdl.handle.net/1807/33493 |
work_keys_str_mv |
AT powandre structuralandfunctionalcharacterizationofclpchaperonesandproteasesinthehumanmalariaparasiteplasmodiumfalciparum |
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