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Functionally critical residues in the aminoglycoside resistance-associated methyltransferase RmtC pl...

Functionally critical residues in the aminoglycoside resistance-associated methyltransferase RmtC pl...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_journals_2266690779

Functionally critical residues in the aminoglycoside resistance-associated methyltransferase RmtC play distinct roles in 30S substrate recognition

About this item

Full title

Functionally critical residues in the aminoglycoside resistance-associated methyltransferase RmtC play distinct roles in 30S substrate recognition

Publisher

Cold Spring Harbor: Cold Spring Harbor Laboratory Press

Journal title

bioRxiv, 2019-10

Language

English

Formats

Publication information

Publisher

Cold Spring Harbor: Cold Spring Harbor Laboratory Press

More information

Scope and Contents

Contents

Methylation of the small ribosome subunit rRNA in the ribosomal decoding center results in exceptionally high-level aminoglycoside resistance in bacteria. Enzymes that methylate 16S rRNA on N7 of nucleotide G1405 (m7G1405) have been identified in both aminoglycoside-producing and clinically drug-resistant pathogenic bacteria. Using a fluorescence p...

Alternative Titles

Full title

Functionally critical residues in the aminoglycoside resistance-associated methyltransferase RmtC play distinct roles in 30S substrate recognition

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_proquest_journals_2266690779

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_journals_2266690779

Other Identifiers

E-ISSN

2692-8205

DOI

10.1101/712810