Zobrazeno 1 - 10
of 32
pro vyhledávání: '"Albert E. Dahlberg"'
Autor:
Frank V. Murphy, Eileen L. Murphy, Jacqueline L. Connetti, Steven T. Gregory, Gerwald Jogl, Hasan DeMirci, Albert E. Dahlberg
Publikováno v:
Antimicrobial Agents and Chemotherapy. 58:4308-4317
Streptomycin is a bactericidal antibiotic that induces translational errors. It binds to the 30S ribosomal subunit, interacting with ribosomal protein S12 and with 16S rRNA through contacts with the phosphodiester backbone. To explore the structural
Autor:
Hasan DeMirci, Venki Ramakrishnan, Albert E. Dahlberg, Steven T. Gregory, Riccardo Belardinelli, Gerwald Jogl, Frank V. Murphy, Ann C. Kelley
Publikováno v:
RNA. 16:2319-2324
All organisms incorporate post-transcriptional modifications into ribosomal RNA, influencing ribosome assembly and function in ways that are poorly understood. The most highly conserved modification is the dimethylation of two adenosines near the 3
Autor:
Albert E. Dahlberg, Gerwald Jogl, Steven T. Gregory, Claudio O. Gualerzi, Riccardo Belardinelli, Hasan DeMirci, Tanakarn Monshupanee
Publikováno v:
RNA. 15:1693-1704
The RsmG methyltransferase is responsible for N7 methylation of G527 of 16S rRNA in bacteria. Here, we report the identification of the Thermus thermophilus rsmG gene, the isolation of rsmG mutants, and the solution of RsmG X-ray crystal structures a
Autor:
Albert E. Dahlberg, Jamie H. D. Cate, Barbara S Schuwirth, Cathy W Hau, Gary R. Janssen, Antón Vila-Sanjurjo, J. Michael Day
Publikováno v:
Nature Structural & Molecular Biology. 13:879-886
The prokaryotic ribosome is an important target of antibiotic action. We determined the X-ray structure of the aminoglycoside kasugamycin (Ksg) in complex with the Escherichia coli 70S ribosome at 3.5-A resolution. The structure reveals that the drug
Publikováno v:
Journal of Bacteriology. 187:4804-4812
Structural studies of the ribosome have benefited greatly from the use of organisms adapted to extreme environments. However, little is known about the mechanisms by which ribosomes or other ribonucleoprotein complexes have adapted to functioning und
Publikováno v:
Nucleic Acids Research. 32:3220-3227
Ribosomal protein L11 and its associated binding site on 23S rRNA together comprise one of the principle components that mediate interactions of translation factors with the ribosome. This site is also the target of the antibiotic thiostrepton, which
A conformational change in the ribosomal peptidyl transferase center upon active/inactive transition
Publikováno v:
Proceedings of the National Academy of Sciences. 98:10096-10101
The ribosome is a dynamic particle that undergoes many structural changes during translation. We show through chemical probing with dimethyl sulfate (DMS) that conformational changes occur at several nucleotides in the peptidyl transferase center upo
Publikováno v:
RNA. 7:969-978
IF3 is essential for ensuring the fidelity of the initiation step of translation in bacterial cells. Mutations at residues R99 and R131 in the C-terminal domain of the factor have previously been shown to increase initiation from the non-canonical GU
Publikováno v:
Journal of Molecular Biology. 309:333-338
We have isolated spontaneous streptomycin-resistant, streptomycin-dependent and streptomycin-pseudo-dependent mutants of the thermophilic bacterium Thermus thermophilus IB-21. All mutant phenotypes were found to result from single amino acid substitu
Publikováno v:
Journal of Molecular Biology. 308:457-463
Interactions within the decoding center of the 30 S ribosomal subunit have been investigated by constructing all 15 possible mutations at nucleotides C1402 and A1500 in helix 44 of 16 S rRNA. As expected, most of the mutations resulted in highly dele