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

Laís Lisboa Corrêa | Zendy; Marta A. Witek | Zendy; Natalia Zelinskaya | Zendy; Renata Cristina Picão | Zendy; Graeme L. Conn | Zendy

Open Access

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

Author(s) -

Laís Lisboa Corrêa,

Marta A. Witek,

Natalia Zelinskaya,

Renata Cristina Picão,

Graeme L. Conn

Publication year - 2015

Publication title -

antimicrobial agents and chemotherapy

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.07

H-Index - 259

eISSN - 1070-6283

pISSN - 0066-4804

DOI - 10.1128/aac.02482-15

Subject(s) - methyltransferase , biology , methylation , heterologous , heterologous expression , escherichia coli , recombinant dna , o methyltransferase , ribosomal rna , aminoglycoside , biochemistry , microbiology and biotechnology , dna , gene , antibiotics

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.

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