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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:
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
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
Autor:
Albert E. Dahlberg, E.A. De Stasio
Publikováno v:
Journal of Molecular Biology. 212:127-133
Eleven of 15 possible single and double mutations were constructed in a cloned copy of Escherichia coli 16 S rDNA at a base-paired site, 1409-1491. Expression of any of these mutations was detrimental to the growth of E. coli. Mutations that substitu