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Figure 4 | Malaria Journal

Figure 4

From: Organization of Plasmodium falciparum spliceosomal core complex and role of arginine methylation in its assembly

Figure 4

Plasmodium SMN protein interacts with PfSmD1 in methylation dependent manner. (A) PfSMN interacts with PfSmD1 protein; (i) Coomassie stained SDS-PAGE gel of purified recombinant GST-PfSMN fusion protein; (ii) GST-PfSMN and GST were immobilized on glutathione sepharose beads. The immobilized proteins were incubated with in vitro translated, [35S] -labelled PfSmD1, PfSmD3 and PfSmB. Bound proteins were eluted by boiling in loading buffer, resolved by SDS-PAGE, visualized by autoradiography of the dried gel. 25% input of the [35S]-labelled proteins are shown. GST served as negative control. (B) Interaction of PfSMN and Tudor domain of PfTSN (PfTu-TSN) with PfSmD1 is methylation dependent. [35S]-methionine-labelled PfSmD1 protein was synthesized using the reticulocyte lysate system, in the presence or absence of the protein methyltransferase inhibitor, Adenosine periodates (AdOx) and incubated with either GST-PfSMN or PfTu-TSN. The interacting proteins were resolved on SDS-PAGE and detected by fluorography. (C) Sequence alignment of Tudor domain of PfSMN like protein with the Tudor domain of human hsSMN homologue. The well-conserved aromatic residues are outlined by reverse red print. (D) Molecular modelling of Tudor domain of PfSMN. Ribbon diagram (upper panel) as well as electrostatic potentials (lower panel) of the homology model of PfSMN compared with human SMN protein. The putative aromatic residues side chains are depicted in stick form. Similar to human SMN Tudor domain, the conserved aromatic residues of Tudor domain of PfSMN-like protein forms aromatic cage implicated in binding of methylated ligands.

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