FASEB J.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Full Text (PDF)
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 Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Pinard, R.
Right arrow Articles by Brakier-Gingras, L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Pinard, R.
Right arrow Articles by Brakier-Gingras, L.

The FASEB Journal, Vol 7, 173-176, Copyright © 1993 by The Federation of American Societies for Experimental Biology

RESEARCH COMMUNICATIONS

The 5' proximal helix of 16S rRNA is involved in the binding of streptomycin to the ribosome

R Pinard, C Payant, P Melancon and L Brakier-Gingras
Departement de Biochimie, Universite de Montreal, Quebec, Canada.

Single mutations at the end of the 5' proximal helix and in the 915 region (13U-->A or C; 914A-->U or G), and double mutations (13U-->A and 914A-->U; 13U-->C and 914A-->G) were constructed into Escherichia coli 16S ribosomal RNA. The mutations were introduced into an expression plasmid containing the rrnB operon under the transcriptional control of the temperature-inducible lambda PL promoter. None of the mutant 16S rRNAs affected cell growth when expressed. Ribosomes extracted after induction of expression of the mutant 16S rRNAs were assayed for their capacity to bind the error-inducing drug streptomycin and for translational misreading in the presence of streptomycin. All mutations impaired the binding of streptomycin, and consequently its capacity to stimulate misreading. Our results demonstrate the involvement of the 5' proximal helix of 16S rRNA in the binding of streptomycin and confirm the participation of the 915 region. They do not support a previous suggestion [Leclerc, D. and Brakier-Gingras, L. (1991) FEBS Lett., Vol. 279, pp. 171-174] that base pairing between nucleotides 13 and 914 stabilizes the binding of streptomycin.


This article has been cited by other articles:


Home page
 RNAHome page
F. BELANGER, G. THEBERGE-JULIEN, P. R. CUNNINGHAM, and L. BRAKIER-GINGRAS
A functional relationship between helix 1 and the 900 tetraloop of 16S ribosomal RNA within the bacterial ribosome
RNA, June 1, 2005; 11(6): 906 - 913.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
J. C. Lee, C. L. Turgeon, and L.-C. C. Yeh
The Accessibility of Yeast Ribosomal Protein L1 as Probed by Proteolysis and Site-directed Mutagenesis Is Different in Intact 60 and 80 S Ribosome
J. Biol. Chem., March 29, 1996; 271(13): 7429 - 7434.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
E. R. Smith and A. H. Merrill , Jr.
Differential Roles of de Novo Sphingolipid Biosynthesis and Turnover in the ``Burst'' of Free Sphingosine and Sphinganine, and Their 1-Phosphates and N-Acyl-Derivatives, That Occurs upon Changing the Medium of Cells in Culture
J. Biol. Chem., August 11, 1995; 270(32): 18749 - 18758.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1993 by The Federation of American Societies for Experimental Biology.