Literature DB >> 3271444

Extension of Watson's model for the elongation cycle of protein biosynthesis.

S V Kirillov1.   

Abstract

The scheme for the elongation cycle of protein biosynthesis is proposed based on modern quantitative data on the interactions of mRNA and different functional forms of tRNA with 70S ribosomes and their 30S and 50S subunits. This scheme takes into account recently discovered third ribosomal (E) site with presumable exit function. The E site is introduced into 70S ribosome by its 50S subunit, the codon-anticodon interaction does not take place at the E site, and the affinity of tRNA for the E site is considerably lower than that for the P site. On the other hand, the P and A sites are located mainly on a 30S subunit, the codon-anticodon interactions being realized on both these sites. An mRNA molecule is placed exclusively on a 30S subunit where it makes U-turn. The proposed scheme does not contradict to any data but includes all main postulates of the initial Watson's model (J. D. Watson, Bull. Soc. Chim. Biol. 46, 1399 (1964), and is considered as a natural extension of the later according to modern experimental data.

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Year:  1986        PMID: 3271444     DOI: 10.1080/07391102.1986.10506345

Source DB:  PubMed          Journal:  J Biomol Struct Dyn        ISSN: 0739-1102


  2 in total

1.  The "allosteric three-site model" of elongation cannot be confirmed in a well-defined ribosome system from Escherichia coli.

Authors:  Y P Semenkov; M V Rodnina; W Wintermeyer
Journal:  Proc Natl Acad Sci U S A       Date:  1996-10-29       Impact factor: 11.205

2.  Influence of systematic error on the shape of the scatchard plot of tRNAPhe binding to eukaryotic ribosomes.

Authors:  S A Nekhai; V E Beletzkij; D M Graifer
Journal:  Biochem J       Date:  1997-07-15       Impact factor: 3.857

  2 in total

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