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

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 mod...

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Bibliographic Details
Published in:Antimicrobial agents and chemotherapy 2016-01, Vol.60 (1), p.699-702
Main Authors: Corrêa, Laís L, Witek, Marta A, Zelinskaya, Natalia, Picão, Renata C, Conn, Graeme L
Format: Article
Language:English
Subjects:
Aminoglycosides - pharmacology
Anti-Bacterial Agents - pharmacology
Bacterial Proteins
Bacterial Proteins - chemistry
Bacterial Proteins - genetics
Bacterial Proteins - metabolism
Cloning, Molecular
Drug Resistance, Bacterial
Drug Resistance, Bacterial - genetics
Escherichia coli
Escherichia coli - drug effects
Escherichia coli - enzymology
Escherichia coli - genetics
Gene Expression
Isoenzymes - chemistry
Isoenzymes - genetics
Isoenzymes - metabolism
Kinetics
Klebsiella pneumoniae - enzymology
Klebsiella pneumoniae - genetics
Mechanisms of Resistance
Methyltransferases
Methyltransferases - chemistry
Methyltransferases - genetics
Methyltransferases - metabolism
Pseudomonas aeruginosa - enzymology
Pseudomonas aeruginosa - genetics
Recombinant Proteins - chemistry
Recombinant Proteins - genetics
Recombinant Proteins - metabolism
S-Adenosylhomocysteine
S-Adenosylhomocysteine - chemistry
S-Adenosylhomocysteine - metabolism
S-Adenosylmethionine
S-Adenosylmethionine - chemistry
S-Adenosylmethionine - metabolism
Substrate Specificity
Transgenes
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Summary: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.
ISSN:0066-4804
1098-6596
DOI:10.1128/AAC.02482-15