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image/svg+xml Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Closed Access logo, derived from PLoS Open Access logo. This version with transparent background. http://commons.wikimedia.org/wiki/File:Closed_Access_logo_transparent.svg Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Journal of Molecular...arrow_drop_down
image/svg+xml Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Closed Access logo, derived from PLoS Open Access logo. This version with transparent background. http://commons.wikimedia.org/wiki/File:Closed_Access_logo_transparent.svg Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao
Journal of Molecular Biology
Article . 1968 . Peer-reviewed
License: Elsevier TDM
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Stability of the messenger RNA-transfer RNA-ribosome complex

Authors: J. Dondon; A.M. Michelson; M. Grunberg-Manago; Grady F. Saunders; C. S. McLaughlin;

Stability of the messenger RNA-transfer RNA-ribosome complex

Abstract

Abstract The thermal stability of the mRNA-aminoacyl-tRNA-ribosome complex and each of its individual components was examined. A temperature-dependent, reversible dissociation of the mRNA-tRNA-ribosome complex has been demonstrated. By analogy with polynucleotide melting curves, the dissociation of the mRNA-tRNA-ribosome complex is considered as a pseudo-phase transition characterized by a melting temperature, T m . The nature of all three components of the complex affects the T m values. The following factors in the mRNA component were demonstrated to influence the T m of the complex: composition of the codon, the non-codon bases, the chain length, and the position of the terminal phosphate group. A comparison of T m values of the complex for tRNA molecules containing only A–U base pairs in their codon-anticodons indicates that regions of the tRNA molecules outside the anticodon may influence the stability of the complex. The source of the ribosomes modifies the T m of the complex, while the method of preparation of the ribosomes appears to have no effect. The mRNA (trinucleotide)-tRNA-ribosome complex is almost 40 °C more stable than the corresponding trinucleotide-polynucleotide complex in the same buffer.

Keywords

Carbon Isotopes, Hot Temperature, Reticulocytes, Nucleotides, Bacillus, RNA, Transfer, Thermography, Escherichia coli, Methods, Animals, RNA, RNA, Messenger, Rabbits, Amino Acids, Ribosomes, Ultracentrifugation

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citations
This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Citations provided by BIP!
popularity
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
BIP!Popularity provided by BIP!
influence
This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Influence provided by BIP!
impulse
This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
BIP!Impulse provided by BIP!
39
Average
Top 10%
Top 10%
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