Skip Navigation

This Article
Right arrow Print PDF (404K)
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 (12)
Right arrowRequest Permissions
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Krzyzosiak, W.J.
Right arrow Articles by Ciesiolka, J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Krzyzosiak, W.J.
Right arrow Articles by Ciesiolka, J.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 1983, Vol. 11, No. 19 6913-6921
© 1983

CHEMISTRY

Long-range conformational trasition in yeast tRNAPhe, induced by the Y-base removal and detected by chloroacetaldehyde modification

W.J. Krzyzosiak+ and J. Ciesiolka

Institute of Bioorganic Chemistry, Polish Academy of Sciences 61-704 Poznan, Noskowskiego 12/14, Poland

+To whom all correspondence should be addressed

Received June 10, 1983. Revised August 19, 1983. Accepted August 19, 1983.

Chemical modification was used to study the conformational changes occuring in yeast tRNAPhe after the Y-base excision. The chemical probe was the adenine- and cytosine-specific reagent chloroacetaldehyde. Comparison of the modification patterns in tRNAPhe and tRNAPhe–Y shows that seven bases, adenines 35, 36 and 38 in the anticodon loop and adenines 73, 76 and cytoaines 74, 75 in the 3'-terminus were modified in both tRNAs with a quantitative difference in the modification level of the anticodon loop bases. The most interesting, however, is the qualitative difference consisting in modification of cytosine-60 in the TYC loop of tRNAPhe–Y. Some aspects of the mechanism of this long-distance conformational transition are briefly discussed.


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
W. F. Waas, Z. Druzina, M. Hanan, and P. Schimmel
Role of a tRNA Base Modification and Its Precursors in Frameshifting in Eukaryotes
J. Biol. Chem., September 7, 2007; 282(36): 26026 - 26034.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
W. F. Waas, V. de Crecy-Lagard, and P. Schimmel
Discovery of a Gene Family Critical to Wyosine Base Formation in a Subset of Phenylalanine-specific Transfer RNAs
J. Biol. Chem., November 11, 2005; 280(45): 37616 - 37622.
[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.