Skip Navigation

This Article
Right arrow Print PDF (642K)
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 (47)
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Desgrès, J.
Right arrow Articles by Gehrke, C. W.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Desgrès, J.
Right arrow Articles by Gehrke, C. W.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 1989, Vol. 17, No. 3 865-882
© 1989

MOLECULAR BIOLOGY

Presence of phosphorylated O-ribosyl-adenosine In T-{psi}-stem of yeast methlonine initiator tRNA

Jean Desgrès, Gérard Keith1, Kenneth C. Kuo2 and Charles W. Gehrke2

Laboratoire de Biochimie Médicale, Université de Bourgogne 21034 Dijon 1Institut de Biologie Moléculaire et Cellulaire du CNRS 67084 Strasbourg, France 2Department of Biochemistry, University of Missouri Columbia, MO 65211, USA

Received December 13, 1988. Accepted January 13, 1989.

We report in this paper on isolation and characterization of two unknown nucleosides G* and [A*] located in the T-{psi}-stem of yeast methionine initiator tRNA, using the combined means of HPLC protocols, real time UV-absorption spectrum, and post-run mass spectrometry by electron impact or fast atom bombardment. The G* nucleoside in position 65 was identified as unmodified guanosine. The structure of the unknown [A*] in position 64 was characterized as an isomeric form of O-ribosyl-adenosine by comparison of its chromatographic, UV-spectral and mass spectrometric properties with those of authentic O-{alpha}-ribofuranosyl-(1->2)-adenosine isolated from biosynthetic poly(adenosine diphosphate ribose). Our studies also brought evidence for the presence of a phosphorylmonoester group located on this new modified nucleoside [A*], when isolated by ion exchange chromatography from enzymic hydrolysis of yeast initiator tRNAMet without phosphatase treatment.


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
 J. Biol. Chem.Home page
A. Stortchevoi, U. Varshney, and U. L. RajBhandary
Common Location of Determinants in Initiator Transfer RNAs for Initiator-Elongator Discrimination in Bacteria and in Eukaryotes
J. Biol. Chem., May 9, 2003; 278(20): 17672 - 17679.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. Biol.Home page
H. J. Drabkin, M. Estrella, and U. L. Rajbhandary
Initiator-Elongator Discrimination in Vertebrate tRNAs for Protein Synthesis
Mol. Cell. Biol., March 1, 1998; 18(3): 1459 - 1466.
[Abstract] [Full Text]

Home page
 J. Biol. Chem.Home page
T. Caldas, E. Binet, P. Bouloc, A. Costa, J. Desgres, and G. Richarme
The FtsJ/RrmJ Heat Shock Protein of Escherichia coli Is a 23 S Ribosomal RNA Methyltransferase
J. Biol. Chem., May 26, 2000; 275(22): 16414 - 16419.
[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.