Characterization of a Plasmodium falciparum rRNA methyltransferase

Publication date: July 2018Source: Molecular and Biochemical Parasitology, Volume 223Author(s): Kirti Gupta, Ankit Gupta, Saman HabibAbstractThe ribosomal RNA adenine dimethyltransferases (rAD) of KsgA/Dim1 family are universally conserved with eukaryotic rADs separated into distinct cytosolic Dim1 and organellar KsgA/TFB homologs. Among the two putative KsgA proteins encoded by the Plasmodium falciparum genome, we found that PfKsgA1 was dually localised in the cytoplasm and the mitochondrion. The protein interacted specifically with small ribosomal subunit as detected by ribosome pull-down using anti-PfKsgA1 antibodies. Recombinant PfKsgA1 exhibited methyltransferase activity which was further confirmed by complementation in an Escherichia coli KsgA knockout strain. Similar to the human mitochondrial KsgA homologs that can additionally function as transcription regulators, PfKsgA1 also interacted with DNA in a sequence non-specific manner suggesting more than one functional role of an important ribosome biogenesis protein in Plasmodium.Graphical abstractA KsgA/Dim1 homolog, PfKsgA1, is dually localised in the cytoplasm and mitochondrion of Plasmodium falciparum. It interacts with the ribosome, methylates adenines on SSU rRNA and complements bacterial KsgA function.
Source: Molecular and Biochemical Parasitology - Category: Parasitology Source Type: research