Skip Navigation

This Article
Right arrow Print PDF (385K)
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 Kersten, H.
Right arrow Articles by Dirheimer, G.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Kersten, H.
Right arrow Articles by Dirheimer, G.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 1978, Vol. 5, No. 8 3033-3042
© 1978

Articles

Recognition of individual procaryotic and eucaryotic transfer-ribonucleic acids by B. subtilis adenine-1-methyltransferase specific for the dihydrouridine loop

H. Kersten, R. Raettig, J. Weissenbach+ and G. Dirheimer+

Institut far Physiologische Chemie Wasserturmstrasse 5, 8520 Erlangen, GFR +Inst. Biol. Mol. et Cell du C.N.R.S., 15, rue Descartes and Fac. Pharm., Univ. Louis Pasteur Strasbourg, France

Received April 7, 1978. Bulk tRNA from yeast and Rat liver can be methylated in vitro with S-adenosylmethionine and B, subtilis extracts. The sole product formed is 1-methyladenosine (m1A). This tRNA (adenine-1) methyl transf erase converts quantitatively the 3'-terminal adenosine-residue in the dihydrouridineloop of tRNAThr and tRNATyr frOm yeast into m1A. Out of 16 eucaryotic tRNAs with known sequences 6 accepted methyl groups, all at a molar ratio of 1. These tRNAs have in common an unpaired adenosine-residue at the specific site in the sequence Py-A-A+-G-G-C-FormulaG, Out of 12 tRNAs from E. coli 6 served as specific substrates. These E. coli tRNAs also have an unpaired adenosine-residue at the 3'-end of the D-loop. Besides restrictions in primary structure intact secondary and tertiary structure is important for recognition of the specific tRNAs by the enzyme.


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
 Nucleic Acids ResHome page
M. Roovers, K. H. Kaminska, K. L. Tkaczuk, D. Gigot, L. Droogmans, and J. M. Bujnicki
The YqfN protein of Bacillus subtilis is the tRNA: m1A22 methyltransferase (TrmK)
Nucleic Acids Res., June 1, 2008; 36(10): 3252 - 3262.
[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.