Zobrazeno 1 - 10
of 23
pro vyhledávání: '"Albert E. Dahlberg"'
Autor:
Wipa Chungjatupornchai, Tanakarn Monshupanee, Albert E. Dahlberg, Stephen Douthwaite, Steven T. Gregory
Publikováno v:
Monshupanee, T, Gregory, S T, Douthwaite, S, Chungjatupornchai, W & Dahlberg, A E 2008, ' Mutations in conserved helix 69 of 23S rRNA of Thermus thermophilus that affect capreomycin resistance but not posttranscriptional modifications ', Journal of Bacteriology, vol. 190, no. 23, pp. 7754-7761 . https://doi.org/10.1128/JB.00984-08
Translocation during the elongation phase of protein synthesis involves the relative movement of the 30S and 50S ribosomal subunits. This movement is the target of tuberactinomycin antibiotics. Here, we describe the isolation and characterization of
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:
RNA. 10:28-33
A mechanistic understanding of ribosome function demands knowledge of the conformational changes that occur during protein synthesis. One current model proposes a conformational switch in Helix 27 (H27) of 16S rRNA involved in the decoding of mRNA. T
Publikováno v:
Journal of Molecular Biology. 319:27-35
The bacterial translational GTPases (initiation factor IF2, elongation factors EF-G and EF-Tu and release factor RF3) are involved in all stages of translation, and evidence indicates that they bind to overlapping sites on the ribosome, whereupon GTP
Autor:
Mark A. Bayfield, Rachel Green, Daniel F. Kim, Steven T. Gregory, Albert E. Dahlberg, Kate R. Lieberman, Jill Thompson, Harry F. Noller, Michael O'Connor
Publikováno v:
Proceedings of the National Academy of Sciences. 98:9002-9007
On the basis of the recent atomic-resolution x-ray structure of the 50S ribosomal subunit, residues A2451 and G2447 of 23S rRNA were proposed to participate directly in ribosome-catalyzed peptide bond formation. We have examined the peptidyltransfera
Publikováno v:
RNA. 6:1166-1173
The translocation stage of protein synthesis is a highly conserved process in all cells. Although the components necessary for translocation have been delineated, the mechanism of this activity has not been well defined. Ribosome movement on template
Autor:
Albert E. Dahlberg, Steven T. Gregory
Publikováno v:
Journal of Molecular Biology. 289:827-834
We have used chemical modification to examine the conformation of 23 S rRNA in Escherichia coli ribosomes bearing erythromycin resistance mutations in ribosomal proteins L22 and L4. Changes in reactivity to chemical probes were observed at several nu
Autor:
Albert E. Dahlberg, Michael O'Connor
Publikováno v:
Journal of Molecular Biology. 254:838-847
The role of ribosomal RNA in maintaining the accuracy of translation has been investigated genetically by selecting for rRNA mutations that promoted frameshifting at a specific site in a reporter gene in Escherichia coli. Mutations were recovered in
Autor:
Albert E. Dahlberg, W. E. Tapprich
Publikováno v:
The EMBO Journal. 9:2649-2655
A single base substitution mutation from guanine to cytosine was constructed at position 2661 of Escherichia coli 23S rRNA and cloned into the rrnB operon of the multi-copy plasmid pKK3535. The mutant plasmid was transformed into E.coli to determine