Natalia Zelinskaya
YOU?
Author Swipe
View article: Mechanism of 30S subunit recognition and modification by the conserved bacterial ribosomal RNA methyltransferase RsmI
Mechanism of 30S subunit recognition and modification by the conserved bacterial ribosomal RNA methyltransferase RsmI Open
Ribosomal RNA (rRNA) modifications are important for ribosome function and can influence bacterial susceptibility to ribosome-targeting antibiotics. The universally conserved 16S rRNA nucleotide C1402, for example, is the only 2’- O -methy…
View article: Basis for selective drug evasion of an aminoglycoside-resistance ribosomal RNA modification
Basis for selective drug evasion of an aminoglycoside-resistance ribosomal RNA modification Open
Aminoglycosides disrupt the fidelity of bacterial protein synthesis, but their potent antibacterial activity is threatened by multiple resistance mechanisms, including methylation of their ribosomal RNA (rRNA) binding site. However, the im…
View article: Discovery of First-in-Class Inhibitors Targeting a Pathogen-Associated Aminoglycoside-Resistance 16S rRNA Methyltransferase
Discovery of First-in-Class Inhibitors Targeting a Pathogen-Associated Aminoglycoside-Resistance 16S rRNA Methyltransferase Open
Among several distinct mechanisms used by bacteria to circumvent antibiotic stress, a predominant form of resistance to ribosome-targeting compounds is the methylation of their ribosomal RNA (rRNA) binding sites. The acquisition of aminogl…
View article: E. coli 70S ribosome complex (Unmethylated 16S A1408 + arbekacin)
E. coli 70S ribosome complex (Unmethylated 16S A1408 + arbekacin) Open
View article: E. coli 70S ribosome complex (N1-methylated 16S A1408 + arbekacin)
E. coli 70S ribosome complex (N1-methylated 16S A1408 + arbekacin) Open
View article: E. coli 70S ribosome complex (N1-methylated 16S A1408 + G418)
E. coli 70S ribosome complex (N1-methylated 16S A1408 + G418) Open
View article: 81 Basis for aminoglycoside evasion of bacterial antibiotic resistance arising from ribosomal RNA modification
81 Basis for aminoglycoside evasion of bacterial antibiotic resistance arising from ribosomal RNA modification Open
View article: 30S subunit recognition and G1405 modification by the aminoglycoside-resistance 16S ribosomal RNA methyltransferase RmtC
30S subunit recognition and G1405 modification by the aminoglycoside-resistance 16S ribosomal RNA methyltransferase RmtC Open
Acquired ribosomal RNA (rRNA) methylation has emerged as a significant mechanism of aminoglycoside resistance in pathogenic bacterial infections. Modification of a single nucleotide in the ribosome decoding center by the aminoglycoside-res…
View article: 30S subunit recognition and G1405 modification by the aminoglycoside-resistance 16S ribosomal RNA methyltransferase RmtC
30S subunit recognition and G1405 modification by the aminoglycoside-resistance 16S ribosomal RNA methyltransferase RmtC Open
Acquired ribosomal RNA (rRNA) methylation has emerged as a significant mechanism of aminoglycoside resistance in pathogenic bacterial infections. Modification of a single nucleotide in the ribosome decoding center by the aminoglycoside-res…
View article: 50S subunit recognition and modification by the <i>Mycobacterium tuberculosis</i> ribosomal RNA methyltransferase TlyA
50S subunit recognition and modification by the <i>Mycobacterium tuberculosis</i> ribosomal RNA methyltransferase TlyA Open
Significance The bacterial ribosome is an important target for antibiotics used to treat infection. However, resistance to these essential drugs can arise through changes in ribosomal RNA (rRNA) modification patterns through the action of …
View article: 50S subunit recognition and modification by the <i>Mycobacterium tuberculosis</i> ribosomal RNA methyltransferase TlyA
50S subunit recognition and modification by the <i>Mycobacterium tuberculosis</i> ribosomal RNA methyltransferase TlyA Open
Changes in bacterial ribosomal RNA methylation status can alter the activity of diverse groups of ribosome-targeting antibiotics. These modifications are typically incorporated by a single methyltransferase that acts on one nucleotide targ…
View article: Functionally critical residues in the aminoglycoside resistance-associated methyltransferase RmtC play distinct roles in 30S substrate recognition
Functionally critical residues in the aminoglycoside resistance-associated methyltransferase RmtC play distinct roles in 30S substrate recognition Open
View article: Functionally critical residues in the aminoglycoside resistance-associated methyltransferase RmtC play distinct roles in 30S substrate recognition
Functionally critical residues in the aminoglycoside resistance-associated methyltransferase RmtC play distinct roles in 30S substrate recognition Open
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 (m 7 G1405) have been iden…
View article: Pseudomonas aeruginosa EftM Is a Thermoregulated Methyltransferase
Pseudomonas aeruginosa EftM Is a Thermoregulated Methyltransferase Open
Pseudomonas aeruginosa is a Gram-negative opportunistic pathogen that trimethylates elongation factor-thermo-unstable (EF-Tu) on lysine 5. Lysine 5 methylation occurs in a temperature-dependent manner and is generally only seen when P. aer…
View article: Heterologous Expression and Functional Characterization of the Exogenously Acquired Aminoglycoside Resistance Methyltransferases RmtD, RmtD2, and RmtG
Heterologous Expression and Functional Characterization of the Exogenously Acquired Aminoglycoside Resistance Methyltransferases RmtD, RmtD2, and RmtG Open
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 a…
View article: The Pathogen-Derived Aminoglycoside Resistance 16S rRNA Methyltransferase NpmA Possesses Dual m <sup>1</sup> A1408/m <sup>1</sup> G1408 Specificity
The Pathogen-Derived Aminoglycoside Resistance 16S rRNA Methyltransferase NpmA Possesses Dual m <sup>1</sup> A1408/m <sup>1</sup> G1408 Specificity Open
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 m 1 A1408/m 1 G1408 activity, an unexpected…
View article: 30S Subunit-Dependent Activation of the Sorangium cellulosum So ce56 Aminoglycoside Resistance-Conferring 16S rRNA Methyltransferase Kmr
30S Subunit-Dependent Activation of the Sorangium cellulosum So ce56 Aminoglycoside Resistance-Conferring 16S rRNA Methyltransferase Kmr Open
Methylation of bacterial 16S rRNA within the ribosomal decoding center confers exceptionally high resistance to aminoglycoside antibiotics. This resistance mechanism is exploited by aminoglycoside producers for self-protection while functi…