The multifaceted histone chaperone RbAp46/48 in Plasmodium falciparum: structural insights, production, and characterization.

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ID: 109647
2020
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Abstract
RbAp46/RBBP7 and RbAp48/RBBP4 are WD40-repeat histone chaperones and chromatin adaptors that reside in multiple complexes involved in maintenance of chromatin structure. RbAp48 is the essential subunit of the chromatin assembly factor-1 (CAF-1) complex, therefore also named as CAF-1C. A detailed in silico sequence and structure analysis of homologs of RbAp46/48 in Plasmodium falciparum (PF3D7_0110700 and PF3D7_1433300) exhibited conservation of characteristic features in both the protein-seven-bladed WD40 β-propeller conformation and different binding interfaces. A comparative structural analysis highlighted species-specific features of the parasite, yeast, drosophila, and human RbAp46/48. In the present study, we report cloning, expression, and characterization of P. falciparum PF3D7_0110700, a putative RbAp46/48 (PfRbAp46/48). PfRbAp46/48 was cloned into pTEM11 vector in fusion with 6xHistidine tag and over-expressed in Escherichia coli B834 cells. The protein was purified by Ni-NTA followed by gel permeation chromatography. The protein expressed in all the three asexual blood stages and exhibited nuclear localization. We showed direct interaction of the purified rPfRbAp46/48 with the histone H4. These findings further our understanding of RbAp46/48 proteins and role of these proteins in the parasite biology.
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kaushik2020theparasitology Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Kaushik, Manjeri;Nehra, Ashima;Gakhar, Surendra Kumar;Gill, Sarvajeet Singh;Gill, Ritu;
Journal parasitology research
Year 2020
DOI
10.1007/s00436-020-06669-5
URL
Keywords
subcellular localization plasmodium falciparum chromatin remodeling rbap46/48 caf-1c protein expression and purification

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