characterizing the role of putative prohibitins of plasmodium falciparum

Abstract

BACKGROUND Understanding the malaria pathogen, Plasmodium falciparum at the molecular level is quite challenging. As the cellular machinery is highly dynamic, any biological system requires an array of interactions among its molecular partners. Protein – protein interactions and complementation studies of putative proteins and proteins of unknown function are essential techniques in deciphering and assessing its functionality. OBJECTIVE Protein – protein interactions regulates all the living processes in the cells. Exploring the interacting proteins and its networks finds a significant impact on identifying the biological role, understanding the disease and for drug discovery. Moreover, assembly of complexes in the biological systems determines the efficient functioning. Cytochrome c oxidase (complex IV) of respiratory chain is assembled in mitochondria. Shy1, an assembly factor, promotes the complex IV biogenesis through association with different protein modules. Surf1 is the human homologue of Shy1. Mutation in Surf1 leads to severe human disorders.