NDLI: Mutations in 16S rRNA that affect UGA (stop codon)-directed translation termination.

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Mutations in 16S rRNA that affect UGA (stop codon)-directed translation termination.

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Mutations in 16S rRNA that affect UGA (stop codon)-directed translation termination.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Dahlberg, A. E. Göringer, H. U. Hijazi, K. A. Murgola, E. J.
Description	Author Affiliation: Göringer HU ( Max-Planck-Institut für Molekulare Genetik, Abteilung Wittmann, Berlin, Federal Republic of Germany.);
Abstract	Site-directed mutagenesis was performed on a sequence motif within the 3' major domain of Escherichia coli 16S rRNA shown previously to be important for peptide chain termination. Analysis of stop codon suppression by the various mutants showed an exclusive response to UGA stop signals, which was correlated directly with the continuity of one or the other of two tandem complementary UCA sequences (bases 1199-1204). Since no other structural features of the mutated ribosomes were hampered and the translation initiation and elongation events functioned properly, we propose that a direct interaction occurs between the UGA stop codon on the mRNA and the 16S rRNA UCA motif as one of the initial events of UGA-dependent peptide chain termination. These results provide evidence that base pairing between rRNA and mRNA plays a direct role in termination, as it has already been shown to do for initiation and elongation.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	15
Volume Number	88
Language	English
Publisher	National Academy of Sciences
Publisher Date	1991-09-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Codon Genetics Escherichia Coli Mutagenesis, Site-Directed Peptide Chain Termination, Translational RNA, Ribosomal, 16S Models, Structural Molecular Sequence Data Nucleic Acid Conformation Oligonucleotide Probes Plasmids Metabolism Recombinant Proteins Ribosomes Beta-Galactosidase Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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