Verma Garima, Surolia Namita
Molecular Parasitology Laboratory, Molecular Biology and Genetics Unit, Jawaharlal Nehru Centre for Advanced Scientific Research, Jakkur, Bangalore 560064, India.
Molecular Parasitology Laboratory, Molecular Biology and Genetics Unit, Jawaharlal Nehru Centre for Advanced Scientific Research, Jakkur, Bangalore 560064, India.
Mol Biochem Parasitol. 2013 Nov-Dec;192(1-2):21-9. doi: 10.1016/j.molbiopara.2013.11.002. Epub 2013 Dec 6.
The Plasmodium falciparum centromeric histone variant PfCENH3 has been shown to occupy a 4-4.5 kb region on each chromosome, but the experimental demonstration of its structure-function relationship remains unexplored. By functional complementation assays, we report that the C-terminus, specifically the CATD region within the HFD of PfCENH3 is essential in centromere function. Our studies also indicate that the PfCENH3 specific LLAL residues of the CATD region are required for centromere targeting and chromosome segregation. Histone H3 of P. falciparum is not found to complement Cse4p (the yeast homologue of CENH3). We also report the identification of PfCENP-C, another component of the inner kinetochore protein complex and its association with PfCENH3. These studies thus delineate the structural determinants of PfCENH3.
恶性疟原虫着丝粒组蛋白变体PfCENH3已被证明在每条染色体上占据4-4.5 kb的区域，但其结构-功能关系的实验证明仍未得到探索。通过功能互补分析，我们报告PfCENH3的C末端，特别是HFD内的CATD区域在着丝粒功能中至关重要。我们的研究还表明，CATD区域的PfCENH3特异性LLAL残基是着丝粒靶向和染色体分离所必需的。未发现恶性疟原虫的组蛋白H3能补充Cse4p（CENH3的酵母同源物）。我们还报告了对内着丝粒蛋白复合物的另一个组分PfCENP-C的鉴定及其与PfCENH3的关联。因此，这些研究描绘了PfCENH3的结构决定因素。
