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Figure 5 | Malaria Journal

Figure 5

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

Figure 5

The mitotic spindle integrity is maintained by the Pf CENP-C dimerization domain. (A) Confocal images showing the mitotic spindle (green) and the Hoechst stained nucleus (blue) of the mif2-3 and mif2-2 TS mutant cells expressing the Pf CENP-C-NTD, -motif and -DD, region, MIF2p and empty vector alone at 23 and 37°C, respectively. At 23°C, all the mif2-3 TS mutants expressing different constructs show normal spindle structure connecting the nuclear masses across the bud and mother cell. At 37°C, both in mif2-3 and mif2-2 TS mutants except the Pf CENP-C-DD and MIF2p, all the other constructs show abnormal and discontinuous spindles. The spindle morphology (green) is also shown in the insets. The broken spindle in the mif2-3 and mif2-2 TS mutant cells are shown by red arrows in the insets. (B) The confocal images representing the disintegrated mitotic spindle morphologies in mif2-3 and mif2-2 TS mutant cells expressing the Pf CENP-C-DD mutants, Pf CENP-CF1993A, Pf CENP-CF1996A and Pf CENP-CY2069A while Pf CENP-CN2060A show normal mitotic spindles at 37°C. NTD- N-terminal region; DD-dimerization domain.

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