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The exogenously acquired 16S rRNA methyltransferases RmtD, RmtD2, and RmtG were cloned and heterologously expressed inEscherichia coli , and the recombinant proteins were purified to near homogeneity. Each methyltransferase conferred an aminoglycoside resistance profile consistent with m7 G1405 modification, and this activity was confirmed byin vitro 30S methylation assays. Analyses of protein structure and interaction withS -adenosyl-l -methionine suggest that the molecular mechanisms of substrate recognition and catalysis are conserved across the 16S rRNA (m7 G1405) methyltransferase family.

Heterologous Expression and Functional Characterization of the Exogenously Acquired Aminoglycoside Resistance Methyltransferases RmtD, RmtD2, and RmtG