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

نویسندگان

  • Laís L Corrêa
  • Marta A Witek
  • Natalia Zelinskaya
  • Renata C Picão
  • Graeme L Conn
چکیده

The exogenously acquired 16S rRNA methyltransferases RmtD, RmtD2, and RmtG were cloned and heterologously expressed in Escherichia coli, and the recombinant proteins were purified to near homogeneity. Each methyltransferase conferred an aminoglycoside resistance profile consistent with m(7)G1405 modification, and this activity was confirmed by in vitro 30S methylation assays. Analyses of protein structure and interaction with S-adenosyl-l-methionine suggest that the molecular mechanisms of substrate recognition and catalysis are conserved across the 16S rRNA (m(7)G1405) methyltransferase family.

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عنوان ژورنال:
  • Antimicrobial agents and chemotherapy

دوره 60 1  شماره 

صفحات  -

تاریخ انتشار 2016