The Pathogen-Derived Aminoglycoside Resistance 16S rRNA Methyltransferase NpmA Possesses Dual m 1 A1408/m 1 G1408 Specificity | Zendy

Natalia Zelinskaya | Zendy; Marta A. Witek | Zendy; Graeme L. Conn | Zendy

Open Access

The Pathogen-Derived Aminoglycoside Resistance 16S rRNA Methyltransferase NpmA Possesses Dual m ¹ A1408/m ¹ G1408 Specificity

Author(s) -

Natalia Zelinskaya,

Marta A. Witek,

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.01872-15

Subject(s) - aminoglycoside , pathogen , methyltransferase , dual (grammatical number) , microbiology and biotechnology , biology , antibiotics , genetics , gene , methylation , philosophy , linguistics

Chemical modification of 16S rRNA can confer exceptionally high-level resistance to a diverse set of aminoglycoside antibiotics. Here, we show that the pathogen-derived enzyme NpmA possesses dual m1 A1408/m1 G1408 activity, an unexpected property apparently unique among the known aminoglycoside resistance 16S rRNA (m1 A1408) methyltransferases. Although the biological significance of this activity remains to be determined, such mechanistic variation in enzymes acquired by pathogens has significant implications for development of inhibitors of these emerging resistance determinants.

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