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pro vyhledávání: '"Albert E. Dahlberg"'
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
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:
Proceedings of the National Academy of Sciences. 96:8973-8978
The downstream box (DB) is a sequence element that enhances translation of several bacterial and phage mRNAs. It has been proposed that the DB enhances translation by base pairing transiently to bases 1469–1483 of 16S rRNA, the so-called anti-DB, d
Publikováno v:
Proceedings of the National Academy of Sciences. 86:4927-4931
A single base was mutated from guanine to adenine at position 791 in 16S rRNA in the Escherichia coli rrnB operon on the multicopy plasmid pKK3535. The plasmid-coded rRNA was processed and assembled into 30S ribosomal subunits in E. coli and caused a