Binding induced RNA conformational changes control substrate recognition and catalysis by the thiostrepton resistance methyltransferase (Tsr)

Abstract

Background: Methylation of rRNA is a common resistance mechanism in antibiotic-producing bacteria. Results: Thiostrepton-resistance methyltransferase (Tsr) amino-terminal domain induces RNA substrate conformational changes necessary for catalysis by its carboxyl-terminal domain. Conclusion:RNAstructural reorganization distal from the methylated nucleotide is implicated in specific substrate recognition by Tsr. Significance: RNA substrate structure can directly regulate modification enzyme activity. © 2014 by The American Society for Biochemistry and Molecular Biology, Inc.