Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Albert E. Dahlberg"'
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:
Nucleic acids research. 32(18)
Peptide bond formation, catalyzed by the ribosomal peptidyltransferase, has long been known to be sensitive to monovalent cation concentrations and pH. More recently, we and others have shown that residue A2451 in the peptidyltransferase center of th
Publikováno v:
Nucleic acids research. 29(3)
U2449 is one of many invariant residues in the central loop of domain V of 23S rRNA, a region that constitutes part of the peptidyltransferase center of the ribosome. In Escherichia coli, this U is post-transcriptionally modified to dihydrouridine (D
Publikováno v:
Nucleic acids research. 24(24)
We have introduced the intervening sequence (IVS) from 23S rRNA of the rrnD operon of Salmonella typhimurium into the equivalent position of Escherichia coli 23S rRNA. Salmonella typhimurium 23S rRNA is fragmented due to the RNase III-dependent remov
Autor:
Albert E. Dahlberg, Steven T. Gregory
Publikováno v:
Nucleic acids research. 23(21)
Using a genetic selection for suppressors of a UGA nonsense mutation in trpA, we have isolated a G to A transition mutation at position 1491 in the decoding region of 16S rRNA. This suppressor displayed no codon specificity, suppressing UGA, UAG and
Publikováno v:
Nucleic acids research. 22(3)
We have produced mutations in a cloned Escherichia coli 23S rRNA gene at positions G2252 and G2253. These sites are protected in chemical footprinting studies by the 3' terminal CCA of P site-bound tRNA. Three possible base changes were introduced at