Skip Navigation

This Article
Right arrow Print PDF (1133K)
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 (29)
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Agris, P. F.
Right arrow Articles by Söll, D.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Agris, P. F.
Right arrow Articles by Söll, D.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 1975, Vol. 2, No. 5 691-699
© 1975

Articles

Maturation of a hypermodified nucleoside in transfer RNA

Paul F. Agris, Donald J. Armstrong$, Klaus P. Schäfer and Dieter Söll*

$Institute of Plant Development, Birge Hall, University of Wisconsin Madison, Wisconsin 53706, USA *Department of Molecular Biophysics and Biochemistry, Yale University New Haven, Connecticut 06520

Received March 4, 1975. E. coli C6 rel– met– cys– was cultured in a fully supplemented medium and in media lacking cysteine or methionine. tRNA isolated from the three cultures contained, respectively, a normal complement of modified nucleosides; a deficiency in thiolated nucleosides and a deficiency in methylated nucleosides. Both sulfur-deficient tPNA and methyl-deficient tRNA contained large amounts of N6-({Delta}2-isopentenyl)adenosine and small amounts of the 2-methylthio derivative. Methyl-deficient tRNA contained, in addition a large amount of a cytokinin active, differently modified nucleoside that is believed to be a sulfur derivative of N6-({delta}2-isopentenyl)adenosine. The structure of this compound is unknown. When methyl-deficient tRNA and the precursor to tRNATyr su3$ A25 were enzymatically methylated in vitro, methyl groups were incorporated into derivatives of isopentenyladenosine. These results indicate that the biosynthesis of the 2-methylthio derivative of isopentenyladenosine may occur in a sequential manner, i.e., thiolation of isopentenyladenosine followed by methylation.


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
 Proc. Natl. Acad. Sci. USAHome page
B. P. Anton, L. Saleh, J. S. Benner, E. A. Raleigh, S. Kasif, and R. J. Roberts
RimO, a MiaB-like enzyme, methylthiolates the universally conserved Asp88 residue of ribosomal protein S12 in Escherichia coli
PNAS, February 12, 2008; 105(6): 1826 - 1831.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
F. Pierrel, H. L. Hernandez, M. K. Johnson, M. Fontecave, and M. Atta
MiaB Protein from Thermotoga maritima: CHARACTERIZATION OF AN EXTREMELY THERMOPHILIC tRNA-METHYLTHIOTRANSFERASE
J. Biol. Chem., August 8, 2003; 278(32): 29515 - 29524.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
F. Pierrel, G. R. Bjork, M. Fontecave, and M. Atta
Enzymatic Modification of tRNAs. MiaB IS AN IRON-SULFUR PROTEIN
J. Biol. Chem., April 12, 2002; 277(16): 13367 - 13370.
[Abstract] [Full Text] [PDF]

Home page
 J. Bacteriol.Home page
B. Esberg, H.-C. E. Leung, H.-C. T. Tsui, G. R. Björk, and M. E. Winkler
Identification of the miaB Gene, Involved in Methylthiolation of Isopentenylated A37 Derivatives in the tRNA of Salmonella typhimurium and Escherichia coli
J. Bacteriol., December 1, 1999; 181(23): 7256 - 7265.
[Abstract] [Full Text]


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.