Skip Navigation

This Article
Right arrow Print PDF (1237K)
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 (25)
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Said, B.
Right arrow Articles by Nomura, M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Said, B.
Right arrow Articles by Nomura, M.
Social Bookmarking
 Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 1988, Vol. 16, No. 22 10529-10545
© 1988


MOLECULAR BIOLOGY

Mutational analysis of the L1 binding site of 23S rRNA in Escherichia coli

Boctor Said, James R. Cole* and Masayasu Nomura+

Department of Biological Chemistry, University of California Irvine, CA 92717, USA

*To whom correspondence should be addressed

Received August 19, 1988. Revised October 14, 1988. Accepted October 14, 1988.

The L11 ribosomal protein operon of Escherichia coli contains the genes for L11 and L1 and is feedback regulated by the translational repressor L1. Both the L1 binding site on 23S rRNA and the L1 repressor target site on L11 operon mRNA share similar proposed secondary structures and contain some primary sequence identity. Several site-directed mutations in the binding region of 23S rRNA were constructed and their effects on binding were examined. For in vitro analysis, a filter binding method was used. For in vivo analysis, a conditional expression system was used to overproduce a 23S rRNA fragment containing the L1 binding region, which leads to specific derepression of the synthesis of L11 and L1. Changes in the shared region of the 23S rRNA L1 binding site produced effects on L1 binding similar to those found previously in analysis of corresponding changes in the L11 operon mRNA target site. The results support the hypothesis that r-protein L1 interacts with both 23S rRNA and L11 operon mRNA by recognizing similar features on both RNAs.


+Present Address: Department of Crop and Soil Sciences, Michigan State University, East Lansing, Michigan 48824, USA


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
GeneticsHome page
A. Kraft, C. Lutz, A. Lingenhel, P. Gröbner, and W. Piendl
Control of Ribosomal Protein L1 Synthesis in Mesophilic and Thermophilic Archaea
Genetics, August 1, 1999; 152(4): 1363 - 1372.
[Abstract] [Full Text]


Home page
J. Biol. Chem.Home page
A.-M. Baker and D. E. Draper
Messenger RNA Recognition by Fragments of Ribosomal Protein S4
J. Biol. Chem., September 29, 1995; 270(39): 22939 - 22945.
[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.