Skip Navigation

This Article
Right arrow Print PDF (1473K)
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 Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Chakraburtty, K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Chakraburtty, K.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 1980, Vol. 8, No. 19 4459-4472
© 1980

ENZYMOLOGY

Recognition of E. coli tRNAArg by arginyl tRNA synthetase

Kalpana Chakraburtty

Department of Biochemistry, Medical College of Wisconsin Milwaukee, WI 53225, USA

Received June 26, 1980. Escherichia coli tRNAArg was digested with ribonuclease T1 under restrictive conditions in order to dissect a minimum number of diester bonds. The number of diester bonds cleaved and their locations were determined by phosphorylation of the newly formed 5' hydroxyl groups with [32P] ATP and polynucleotide kinase. There was complete loss of aminoacylation of tRNAArg when two diester bonds were cleaved at the anticodon. However, this material retained the specific properties of synthetase recognition. Two fragments were derived by further digestion of this tRNA. One 19 nucleotide-long fragment derived from the 3' end of tRNAArg and another 18 nucleotide-long fragment derived from the 5' end of the molecule were required to maintain the properties of the specific recognition by the arginyl tRNA synthetase in the absence of the rest of the structure including the anticodon.


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
 ScienceHome page
L. Schulman and H Pelka
The anticodon contains a major element of the identity of arginine transfer RNAs
Science, December 22, 1989; 246(4937): 1595 - 1597.
[Abstract] [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.