A Single RNaseIII Domain Protein from Entamoeba histolytica Has dsRNA Cleavage Activity and Can Help Mediate RNAi Gene Silencing in a Heterologous System
Fig 1
Comparison of RNaseIII proteins.
(A) Schematic of domain structure of Dicer enzymes across organisms including Human Dicer (Accession Q9UPY3), Giardia lamblia Dicer (Accession EDO77862), Trypanosoma brucei Dicer 1 (Accession Tb927.8.2370), Trypanosoma brucei Dicer 2 (Accession Tb927.3.1230), Saccharomyces castellii Dicer 1 (Accession DAA12515), and E. histolytica RNaseIII (EHI_068740). Scale along the bottom indicates the approximate location of each domain. (B) ClustalW alignment of RNaseIII domains across organisms including EhRNaseIII, Escherichia coli RNaseIII (Accession AIL18413), Aquifex aeolicus RNaseIII (Accession NP_213645), S. castellii Dicer1, Arabidopsis thaliana Dicer (Accession AEZ02177), Human Dicer, and Giardia Dicer. Full-length sequences aligned using Geneious version R7 (Biomatters Ltd) [31]. Excerpt of alignment of catalytic residues shown. RNaseIII signature motif is shown in bold. Important catalytic residues are shown in red. Full-length alignment of EhRNaseIII is available in S1 Fig.