Skip Navigation

This Article
Right arrow Print PDF (301K)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (22)
Right arrowRequest Permissions
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Prescott, C.
Right arrow Articles by Nierhaus, K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Prescott, C.
Right arrow Articles by Nierhaus, K.
Social Bookmarking
 Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 1991, Vol. 19, No. 19 5281-5283
© 1991


MOLECULAR BIOLOGY

Ribosomes containing the C1054-deletion mutation in E.coli 16S rRNA act as suppressors at all three nonsense codons

Catherine Prescott, Ludwig Krabben and Knud Nierhaus

Max Planck Institut für Molekulare Genetik Ihnestrasse 73, D-1000 Berlin 33, FRG

Received July 8, 1991. Accepted September 12, 1991.

It was established some time ago that the deletion of base C1054 in E.coli 16S rRNA specifically affects UGAdependent termination of translation. Based on this observation, a model for the termination event was proposed in which the UGA nonsense codon on the mRNA base-pairs with a complementary motif in 'helix 34' of the 16S rRNA, thus potentially providing a recognition signal for the binding of the release factor. This model has been re-examined here and evidence is presented which demonstrates that ribosomes containing the C1054A mutation enhance the activity of suppressors of both UAG and UAA termination codons introduced into the host. The results do not support the nonsense codon-16S rRNA base pairing model, and rather imply a more general involvement of 'helix 34' in the translation termination reactions.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
J. Biol. Chem.Home page
A. Kubarenko, P. Sergiev, W. Wintermeyer, O. Dontsova, and M. V. Rodnina
Involvement of Helix 34 of 16 S rRNA in Decoding and Translocation on the Ribosome
J. Biol. Chem., November 17, 2006; 281(46): 35235 - 35244.
[Abstract] [Full Text] [PDF]


Home page
Microbiol. Mol. Biol. Rev.Home page
M. C. Ganoza, M. C. Kiel, and H. Aoki
Evolutionary Conservation of Reactions in Translation
Microbiol. Mol. Biol. Rev., September 1, 2002; 66(3): 460 - 485.
[Abstract] [Full Text] [PDF]


Home page
Nucleic Acids ResHome page
L. Harrell, U. Melcher, and J. F. Atkins
Predominance of six different hexanucleotide recoding signals 3' of read-through stop codons
Nucleic Acids Res., May 1, 2002; 30(9): 2011 - 2017.
[Abstract] [Full Text] [PDF]



Disclaimer:
Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.