A Novel Motif for S-Adenosyl-l-methionine Binding by the Ribosomal RNA Methyltransferase TlyA from Mycobacterium tuberculosis.

@article{Witek2017ANM,
  title={A Novel Motif for S-Adenosyl-l-methionine Binding by the Ribosomal RNA Methyltransferase TlyA from Mycobacterium tuberculosis.},
  author={Marta A. Witek and Emily G Kuiper and Elizabeth Minten and Emily K. Crispell and Graeme L. Conn},
  journal={The Journal of biological chemistry},
  year={2017},
  volume={292 5},
  pages={1977-1987}
}
Capreomycin is a potent ribosome-targeting antibiotic that is an essential component of current antituberculosis treatments, particularly in the case of multidrug-resistant Mycobacterium tuberculosis (Mtb). Optimal capreomycin binding and Mtb ribosome inhibition requires ribosomal RNA methylation in both ribosome subunits by TlyA (Rv1694), an enzyme with dual 2'-O-methytransferase and putative hemolytic activities. Despite the important role of TlyA in capreomycin sensitivity and identification… CONTINUE READING

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Capreomycin is a potent ribosome - targeting antibiotic that is an essential component of current antituberculosis treatments , particularly in the case of multidrug - resistant Mycobacterium tuberculosis ( Mtb ) .
Capreomycin is a potent ribosome - targeting antibiotic that is an essential component of current antituberculosis treatments , particularly in the case of multidrug - resistant Mycobacterium tuberculosis ( Mtb ) .
RibosomesIs associated anatomy of gene productRibosomal RNA
Optimal capreomycin binding and Mtb ribosome inhibition requires ribosomal RNA methylation in both ribosome subunits by TlyA ( Rv1694 ) , an enzyme with dual 2'-O - methytransferase and putative hemolytic activities .
Optimal capreomycin binding and Mtb ribosome inhibition requires ribosomal RNA methylation in both ribosome subunits by TlyA ( Rv1694 ) , an enzyme with dual 2'-O - methytransferase and putative hemolytic activities .
Optimal capreomycin binding and Mtb ribosome inhibition requires ribosomal RNA methylation in both ribosome subunits by TlyA ( Rv1694 ) , an enzyme with dual 2'-O - methytransferase and putative hemolytic activities .
Optimal capreomycin binding and Mtb ribosome inhibition requires ribosomal RNA methylation in both ribosome subunits by TlyA ( Rv1694 ) , an enzyme with dual 2'-O - methytransferase and putative hemolytic activities .
Optimal capreomycin binding and Mtb ribosome inhibition requires ribosomal RNA methylation in both ribosome subunits by TlyA ( Rv1694 ) , an enzyme with dual 2'-O - methytransferase and putative hemolytic activities .
Optimal capreomycin binding and Mtb ribosome inhibition requires ribosomal RNA methylation in both ribosome subunits by TlyA ( Rv1694 ) , an enzyme with dual 2'-O - methytransferase and putative hemolytic activities .
Optimal capreomycin binding and Mtb ribosome inhibition requires ribosomal RNA methylation in both ribosome subunits by TlyA ( Rv1694 ) , an enzyme with dual 2'-O - methytransferase and putative hemolytic activities .
Optimal capreomycin binding and Mtb ribosome inhibition requires ribosomal RNA methylation in both ribosome subunits by TlyA ( Rv1694 ) , an enzyme with dual 2'-O - methytransferase and putative hemolytic activities .
Optimal capreomycin binding and Mtb ribosome inhibition requires ribosomal RNA methylation in both ribosome subunits by TlyA ( Rv1694 ) , an enzyme with dual 2'-O - methytransferase and putative hemolytic activities .
Capreomycin is a potent ribosome - targeting antibiotic that is an essential component of current antituberculosis treatments , particularly in the case of multidrug - resistant Mycobacterium tuberculosis ( Mtb ) .
Capreomycin is a potent ribosome - targeting antibiotic that is an essential component of current antituberculosis treatments , particularly in the case of multidrug - resistant Mycobacterium tuberculosis ( Mtb ) .
Optimal capreomycin binding and Mtb ribosome inhibition requires ribosomal RNA methylation in both ribosome subunits by TlyA ( Rv1694 ) , an enzyme with dual 2'-O - methytransferase and putative hemolytic activities .
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