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Background  The conserved centromere-associated proteins, CENH3 (or CENP-A) and CENP-C are indispensable for the functional centromere-kinetochore assembly, chromosome segregation, cell cycle progression, and viability. The presence and functions of centromere proteins in  Plasmodium falciparum  are not well studied. Identification of  Pf CENP-C, an inner kinetochore protein (the homologue of human CENP-C) and its co-localization with  Pf CENH3 was recently reported. This study aims to decipher the functions of inner kinetochore protein,  Pf CENP-C as a centromere protein in  P. falciparum .    Methods  Bio-informatic tools were employed to demarcate the two conserved domains of  Pf CENP-C, and the functions of  Pf CENP-C domains were demonstrated by functional complementation assays in the temperature sensitive (TS) mutant strains (mif2-3 and mif2-2) of  Saccharomyces cerevisiae  with MIF2p (the yeast homologue of CENP-C) loss-of-function. By site-directed mutagenesis, the key residues essential for  Pf CENP-C functions were determined. The chromatin immunoprecipitation was carried out to determine the  in vivo  binding of  Pf CENP-C to the  Plasmodium  centromeres and the  in vivo  interactions of  Pf CENP-C with  Pf CENH3, and mitotic spindles were shown by co-immunopreciptation experiments.    Results  The studies demonstrate that the motif and the dimerization domain of  Pf CENP-C is able to functionally complement MIF2p functions. The essential role of some of the key residues: F1993, F1996 and Y2069 within the  Pf CENP-C dimerization domain in mediating its functions and maintenance of mitotic spindle integrity is evident from this study. The pull-down assays show the association of  Pf CENP-C with  Pf CENH3 and mitotic spindles. The ChIP-PCR experiments confirm  Pf CENP-C-enriched  Plasmodium  centromeres. These studies thus provide an insight into the roles of this inner kinetochore protein and establish that the centromere proteins are evolutionary conserved in the parasite.    Conclusions   Pf CENP-C is a true CENP-C homologue in  P. falciparum  which binds to the centromeric DNA and its dimerization domain is essential for its  in vivo  functions as a centromere protein. The identification and functional characterization of the  P. falciparum  centromeric proteins will provide mechanistic insights into some of the mitotic events that occur during the chromosome segregation in human malaria parasite,  P. falciparum .    Electronic supplementary material  The online version of this article (doi:10.1186/1475-2875-13-475) contains supplementary material, which is available to authorized users.

The dimerization domain of Pf CENP-C is required for its functions as a centromere protein in human malaria parasite Plasmodium falciparum