Poulsen, B.R., Nohr, J., Douthwaite, S., Hansen, L.V., Iversen, J.J.L., Visser, J., ...
Many biosynthetic reactions and bioconversions are limited by low availability of NADPH. With the purpose of increasing the NADPH concentration and/or the flux through the pentose phosphate pathway...
Requirement for a conserved, tertiary interaction in the core of 23S ribosomal RNA.
A putative base-pairing interaction that determines the folding of the central region of 23S rRNA has been investigated by mutagenesis. Each of the possible base substitutions has been made at the...
Farrell, D. J., Douthwaite, S., Morrissey, I., Bakker, S., Poehlsgaard, J., Jakobsen, L., ...
Sixteen (1.5%) of the 1,043 clinical macrolide-resistant Streptococcus pneumoniae isolates collected and analyzed in the 1999-2000 PROTEKT (Prospective Resistant Organism Tracking and Epidemiology...
The ErmE methyltransferase from the erythromycin-producing actinomycete Saccharopolyspora erythraea dimethylates the N-6 position of adenine 2058 in domain V of 23S rRNA. This modification confers...
Functional interactions within 23S rRNA involving the peptidyltransferase center.
A molecular genetic approach has been employed to investigate functional interactions within 23S rRNA. Each of the three base substitutions at guanine 2032 has been made. The 2032A mutation confers...
The ribosomal protein L11 binds to the region of 23S rRNA associated with the GTPase-dependent steps of protein synthesis. Nucleotides 1054-1107 within this region of the Escherichia coli 23S rRNA...
Douthwaite, S, Garrett, R A, Wagner, R, Feunteun, J
An RNA fragment, constituting three subfragments of nucleotide sequences 1-11, 69-87 and 89-120, is the most ribonuclease-resistant part of the native 5S RNA of Escherichia coli, at 0 degrees C. A...
Interaction of the antibiotics clindamycin and lincomycin with Escherichia coli 23S ribosomal RNA.
Interaction of the antibiotics clindamycin and lincomycin with Escherichia coli ribosomes has been compared by chemical footprinting. The protection afforded by both drugs is limited to the peptidyl...
A "bulged" double helix in a RNA-protein contact site.
Peattie, D A, Douthwaite, S, Garrett, R A, Noller, H F
The binding of ribosomal protein L18 affects specific nucleotides in Escherichia coli 5S RNA as detected by dimethyl sulfate alkylation and RNase A digestion of the 5S-L18 complex. Most of the...
Douthwaite, S, Prince, J B, Noller, H F
A mutation affording low levels of erythromycin resistance has been obtained by in vitro hydroxylamine mutagenesis of a cloned ribosomal RNA operon from Escherichia coli. The site of the mutational...
Antibiotic interactions at the GTPase-associated centre within Escherichia coli 23S rRNA.
Egebjerg, J, Douthwaite, S, Garrett, R A
A comprehensive range of chemical reagents and ribonucleases was employed to investigate the interaction of the antibiotics thiostrepton and micrococcin with the ribosomal protein L11-23S RNA complex...
The antibiotics thiostrepton and micrococcin bind to the GTPase region in domain II of 23S rRNA, and inhibit ribosomal A-site associated reactions. When bound to the ribosome, these antibiotics alter...
Basis for prokaryotic specificity of action of aminoglycoside antibiotics.
Recht, M I, Douthwaite, S, Puglisi, J D
The aminoglycosides, a group of structurally related antibiotics, bind to rRNA in the small subunit of the prokaryotic ribosome. Most aminoglycosides are inactive or weakly active against eukaryotic...
Vester, B, Hansen, L H, Douthwaite, S
The ErmE methyltransferase confers resistance to MLS antibiotics by specifically dimethylating adenine 2058 (A2058, Escherichia coli numbering) in bacterial 23S rRNA. To define nucleotides in the...
Hansen, L H, Vester, B, Douthwaite, S
Under physiological conditions, the ErmE methyltransferase specifically modifies a single adenosine within ribosomal RNA (rRNA), and thereby confers resistance to multiple antibiotics. The adenosine...
Negative in vitro selection identifies the rRNA recognition motif for ErmE methyltransferase.
Nielsen, A K, Douthwaite, S, Vester, B
Erm methyltransferases modify bacterial 23S ribosomal RNA at adenosine 2058 (A2058, Escherichia coli numbering) conferring resistance to macrolide, lincosamide, and streptogramin B (MLS) antibiotics....
Mapping posttranscriptional modifications in 5S ribosomal RNA by MALDI mass spectrometry.
Kirpekar, F, Douthwaite, S, Roepstorff, P
We present a method to screen RNA for posttranscriptional modifications based on Matrix Assisted Laser Desorption/Ionization mass spectrometry (MALDI-MS). After the RNA is digested to completion with...
Vester, B, Hansen, L H, Douthwaite, S
The ErmE methyltransferase confers resistance to MLS antibiotics by specifically dimethylating adenine 2058 (A2058, Escherichia coli numbering) in bacterial 23S rRNA. To define nucleotides in the...
Requirement for a conserved, tertiary interaction in the core of 23S ribosomal RNA.
A putative base-pairing interaction that determines the folding of the central region of 23S rRNA has been investigated by mutagenesis. Each of the possible base substitutions has been made at the...
Farrell, D. J., Douthwaite, S., Morrissey, I., Bakker, S., Poehlsgaard, J., Jakobsen, L., ...
Sixteen (1.5%) of the 1,043 clinical macrolide-resistant Streptococcus pneumoniae isolates collected and analyzed in the 1999-2000 PROTEKT (Prospective Resistant Organism Tracking and Epidemiology...
The ErmE methyltransferase from the erythromycin-producing actinomycete Saccharopolyspora erythraea dimethylates the N-6 position of adenine 2058 in domain V of 23S rRNA. This modification confers...
Functional interactions within 23S rRNA involving the peptidyltransferase center.
A molecular genetic approach has been employed to investigate functional interactions within 23S rRNA. Each of the three base substitutions at guanine 2032 has been made. The 2032A mutation confers...
The ribosomal protein L11 binds to the region of 23S rRNA associated with the GTPase-dependent steps of protein synthesis. Nucleotides 1054-1107 within this region of the Escherichia coli 23S rRNA...
Douthwaite, S, Garrett, R A, Wagner, R, Feunteun, J
An RNA fragment, constituting three subfragments of nucleotide sequences 1-11, 69-87 and 89-120, is the most ribonuclease-resistant part of the native 5S RNA of Escherichia coli, at 0 degrees C. A...
Interaction of the antibiotics clindamycin and lincomycin with Escherichia coli 23S ribosomal RNA.
Interaction of the antibiotics clindamycin and lincomycin with Escherichia coli ribosomes has been compared by chemical footprinting. The protection afforded by both drugs is limited to the peptidyl...
A "bulged" double helix in a RNA-protein contact site.
Peattie, D A, Douthwaite, S, Garrett, R A, Noller, H F
The binding of ribosomal protein L18 affects specific nucleotides in Escherichia coli 5S RNA as detected by dimethyl sulfate alkylation and RNase A digestion of the 5S-L18 complex. Most of the...
Douthwaite, S, Prince, J B, Noller, H F
A mutation affording low levels of erythromycin resistance has been obtained by in vitro hydroxylamine mutagenesis of a cloned ribosomal RNA operon from Escherichia coli. The site of the mutational...
Antibiotic interactions at the GTPase-associated centre within Escherichia coli 23S rRNA.
Egebjerg, J, Douthwaite, S, Garrett, R A
A comprehensive range of chemical reagents and ribonucleases was employed to investigate the interaction of the antibiotics thiostrepton and micrococcin with the ribosomal protein L11-23S RNA complex...
The antibiotics thiostrepton and micrococcin bind to the GTPase region in domain II of 23S rRNA, and inhibit ribosomal A-site associated reactions. When bound to the ribosome, these antibiotics alter...
Basis for prokaryotic specificity of action of aminoglycoside antibiotics.
Recht, M I, Douthwaite, S, Puglisi, J D
The aminoglycosides, a group of structurally related antibiotics, bind to rRNA in the small subunit of the prokaryotic ribosome. Most aminoglycosides are inactive or weakly active against eukaryotic...
Hansen, L H, Vester, B, Douthwaite, S
Under physiological conditions, the ErmE methyltransferase specifically modifies a single adenosine within ribosomal RNA (rRNA), and thereby confers resistance to multiple antibiotics. The adenosine...
Negative in vitro selection identifies the rRNA recognition motif for ErmE methyltransferase.
Nielsen, A K, Douthwaite, S, Vester, B
Erm methyltransferases modify bacterial 23S ribosomal RNA at adenosine 2058 (A2058, Escherichia coli numbering) conferring resistance to macrolide, lincosamide, and streptogramin B (MLS) antibiotics....
Mapping posttranscriptional modifications in 5S ribosomal RNA by MALDI mass spectrometry.
Kirpekar, F, Douthwaite, S, Roepstorff, P
We present a method to screen RNA for posttranscriptional modifications based on Matrix Assisted Laser Desorption/Ionization mass spectrometry (MALDI-MS). After the RNA is digested to completion with...
Vester, B, Hansen, L H, Douthwaite, S
The ErmE methyltransferase confers resistance to MLS antibiotics by specifically dimethylating adenine 2058 (A2058, Escherichia coli numbering) in bacterial 23S rRNA. To define nucleotides in the...