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Full-Text Articles in Medicine and Health Sciences
Plasmodium Falciparum Hep1 Is Required To Prevent The Self Aggregation Of Pfhsp70-3, D Nyakundi, L Vuko, S Bentley, H Hoppe, G Blatch, A Boshoff
Plasmodium Falciparum Hep1 Is Required To Prevent The Self Aggregation Of Pfhsp70-3, D Nyakundi, L Vuko, S Bentley, H Hoppe, G Blatch, A Boshoff
Health Sciences Papers and Journal Articles
The majority of mitochondrial proteins are encoded in the nucleus and need to be imported from the cytosol into the mitochondria, and molecular chaperones play a key role in the efficient translocation and proper folding of these proteins in the matrix. One such molecular chaperone is the eukaryotic mitochondrial heat shock protein 70 (Hsp70); however, it is prone to self-aggregation and requires the presence of an essential zinc-finger protein, Hsp70-escort protein 1 (Hep1), to maintain its structure and function. PfHsp70-3, the only Hsp70 predicted to localize in the mitochondria of P. falciparum, may also rely on a Hep1 orthologue to …
The Malarial Exported Pfa0660w Is An Hsp40 Co-Chaperone Of Pfhsp70-X, M Daniyan, A Boshoff, E Prinsloo, E Pesce, G Blatch
The Malarial Exported Pfa0660w Is An Hsp40 Co-Chaperone Of Pfhsp70-X, M Daniyan, A Boshoff, E Prinsloo, E Pesce, G Blatch
Medical Papers and Journal Articles
Plasmodium falciparum, the human pathogen responsible for the most dangerous malaria infection, survives and develops in mature erythrocytes through the export of proteins needed for remodelling of the host cell. Molecular chaperones of the heat shock protein (Hsp) family are prominent members of the exportome, including a number of Hsp40s and a Hsp70. PFA0660w, a type II Hsp40, has been shown to be exported and possibly form a complex with PfHsp70-x in the infected erythrocyte cytosol. However, the chaperone properties of PFA0660w and its interaction with human and parasite Hsp70s are yet to be investigated. Recombinant PFA0660w was found to …