Structure of the Escherichia coli ribosomal termination complex with release factor 2-Reference-Cited by-同舟云学术

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Structure of the Escherichia coli ribosomal termination complex with release factor 2

Published:2003-01 Issue:6918 Volume:421 Page:90-94
ISSN:0028-0836
Container-title:Nature
language:en
Short-container-title:Nature

Author:

Klaholz Bruno P.,Pape Tillmann,Zavialov Andrey V.,Myasnikov Alexander G.,Orlova Elena V.,Vestergaard Bente,Ehrenberg Måns,van Heel Marin

Publisher

Springer Science and Business Media LLC

Subject

Multidisciplinary

Link

http://www.nature.com/articles/nature01225.pdf

Reference29 articles.

1. Kisselev, L. L. & Buckingham, R. H. Translational termination comes of age. Trends Biochem. Sci. 25, 561–566 (2000)

2. Ito, K., Uno, M. & Nakamura, Y. A tripeptide ‘anticodon’ deciphers stop codons in messenger RNA. Nature 403, 680–684 (2000)

3. Frolova, L. Y. et al. Mutations in the highly conserved GGQ-motif of class 1 polypeptide release factors abolish ability of human eRF1 to trigger peptidyl-tRNA hydrolysis. RNA 5, 1014–1020 (1999)

4. Zavialov, A. V., Mora, L., Buckingham, R. H. & Ehrenberg, M. Release of peptide promoted by the GGQ-motif of class 1 release factors regulates the GTPase activity of RF3. Mol. Cell (in the press)

5. Song, H. et al. The crystal structure of human eukaryotic release factor eRF1-mechanism of stop codon recognition and peptidyl-tRNA hydrolysis. Cell 100, 311–321 (2000)

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