Skip Navigation

This Article
Right arrow Print PDF (2116K)
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 (18)
Right arrowRequest Permissions
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Bertram, S.
Right arrow Articles by Wagner, R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Bertram, S.
Right arrow Articles by Wagner, R.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 1983, Vol. 11, No. 3 575-589
© 1983

MOLECULAR BIOLOGY

Structure investigation of Phe-tRNAphe from E.coli bound to the ribosomal A-site

S. Bertram, U. Göringer and R. Wagner

Max-Planck-Institut for Molekulare Genetik Abt. Wittmann, Ihnestrasse 63-73, 1000 Berlin-Dahlem, FRG

Received December 20, 1982. Accepted January 11, 1983.

Kethoxal modification of guanosines within phe-tRNAphe from E.Coli was studied for tRNA in the free state and specifically bound to the ribosomal A-site. Complex formation with the ribosome results in a protection from chemical modification of two distant sites in the tRNA molecule. The guanosines affected are G-18 and G-19, located in the D-loop, and G-34 in the anticodon loop.

Modification of phe-tRNAphe in the absence of ribosomes leads to a destabilisation of the tRNA structure. Our data are consistent with the conclusion that mocification of G-34 at the anticodon loop triggers a conformational instability in distant parts of the tRNA molecule.


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
 RNAHome page
L. D. Kapp, S. E. Kolitz, and J. R. Lorsch
Yeast initiator tRNA identity elements cooperate to influence multiple steps of translation initiation
RNA, May 1, 2006; 12(5): 751 - 764.
[Abstract] [Full Text] [PDF]

Home page
 Nucleic Acids ResHome page
I. Amarantos and D. L. Kalpaxis
Photoaffinity polyamines: interactions with AcPhe-tRNA free in solution or bound at the P-site of Escherichia coli ribosomes
Nucleic Acids Res., October 1, 2000; 28(19): 3733 - 3742.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
C. Alexander, N. Bilgin, C. Lindschau, J. R. Mesters, B. Kraal, R. Hilgenfeld, V. A. Erdmann, and C. Lippmann
Phosphorylation of Elongation Factor Tu Prevents Ternary Complex Formation
J. Biol. Chem., June 16, 1995; 270(24): 14541 - 14547.
[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.