Heterologous Expression and Functional Characterization of the Exogenously Acquired Aminoglycoside Resistance Methyltransferases RmtD, RmtD2, and RmtG
| Autor: | Natalia Zelinskaya, Renata Cristina Picão, Marta A. Witek, Graeme L. Conn, Laís Lisboa Corrêa |
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| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
S-Adenosylmethionine Methyltransferase 030106 microbiology Gene Expression Biology medicine.disease_cause Substrate Specificity law.invention 03 medical and health sciences Protein structure Bacterial Proteins Mechanisms of Resistance law Drug Resistance Bacterial Gene expression Escherichia coli medicine Pharmacology (medical) Transgenes Cloning Molecular Pharmacology Cloning Methyltransferases Methylation S-Adenosylhomocysteine Molecular biology Recombinant Proteins Anti-Bacterial Agents Isoenzymes Kinetics Klebsiella pneumoniae Aminoglycosides Infectious Diseases Pseudomonas aeruginosa Recombinant DNA Heterologous expression |
| Zdroj: | Antimicrobial Agents and Chemotherapy. 60:699-702 |
| ISSN: | 1098-6596 0066-4804 |
| DOI: | 10.1128/aac.02482-15 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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