Skip Navigation

This Article
Right arrow Print PDF (1762K)
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 (54)
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Westermann, P.
Right arrow Articles by Bielka, H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Westermann, P.
Right arrow Articles by Bielka, H.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 1981, Vol. 9, No. 10 2387-2396
© 1981

MOLECULAR BIOLOGY

Cross-linking of Met-tRNAf to eIF-2ß and to the ribosomal proteins S3a and S6 within the eukaryotic initiation complex, eIF-2-GMPPCP Met-tRNAf-small ribosomal subunit

Peter Westermann, Odd Nygârd*,+ and Heinz Bielka

Central Institute of Molecular Biology, Academy of Sciences of GDR 1115 Berlin-Buch, GDR *Department of Cell Physiology, The Wenner-Gren Institute, University of Stockholm S-l 13 45 Stockholm, Sweden

+To whom correspondence should be addressed

Received March 12, 1981. In the quaternary initiation complex, eIF-2-GMPPCP-Met-tRNAf-40S ribosomal subunit, the Met-tRNAf can be cross-linked to the B subunit of initiation factor eIF-2 as well as to ribosomal proteins S3a and S6 by treatment with the bifunctional reagent, diepoxybutane. Using 40S subunits, modified in advance with the heterobifunctional reagent, methyl-p-azido-benzoylaminoacetimidate, Met-tRNAf is covalently bound to the same ribosomal proteins (S3a and S6) upon irradiation of the complex with ultraviolet light. Under both conditions proteins S3a and S6, together with a limited number of other ribosomal proteins, are covalently bound to 18S ribosomal RNA.


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
 GeneticsHome page
J. W. Loar, R. M. Seiser, A. E. Sundberg, H. J. Sagerson, N. Ilias, P. Zobel-Thropp, E. A. Craig, and D. E. Lycan
Genetic and Biochemical Interactions Among Yar1, Ltv1 and RpS3 Define Novel Links Between Environmental Stress and Ribosome Biogenesis in Saccharomyces cerevisiae
Genetics, December 1, 2004; 168(4): 1877 - 1889.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
K. Cui, M. Coutts, J. Stahl, and A. J. Sytkowski
Novel Interaction between the Transcription Factor CHOP (GADD153) and the Ribosomal Protein FTE/S3a Modulates Erythropoiesis
J. Biol. Chem., March 10, 2000; 275(11): 7591 - 7596.
[Abstract] [Full Text] [PDF]

Home page
 J. Cell Biol.Home page
H. Naora, I. Takai, M. Adachi, and H. Naora
Altered Cellular Responses by Varying Expression of a Ribosomal Protein Gene: Sequential Coordination of Enhancement and Suppression of Ribosomal Protein S3a Gene Expression Induces Apoptosis
J. Cell Biol., May 4, 1998; 141(3): 741 - 753.
[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.