Literature DB >> 3889832

The secondary structure of mRNAs from Escherichia coli: its possible role in increasing the accuracy of translation.

E G Shpaer.   

Abstract

A secondary structure model was proposed for mRNAs during translation (in a polysome) where the secondary structure is described by a set of small unbranched hairpins. Computer simulation experiments reveal that the number of hairpins is much greater (P less than 10(-6) in highly expressed mRNAs from E. coli as compared with the random sequences coding for the same amino acid sequence, i.e. certain synonymous codons are used in definite mRNA positions to increase the number of hairpins. No constraints on the amino acid sequence, which would affect the secondary structure of mRNAs, were found. The codons UGU, UGC (Cys), GCC (Ala), ACA, ACG (Thr), CCU, CCC (Pro), etc. translated by minor tRNAs were found to occur significantly more frequently in the position 5' to the hairpins than the other codons translated by major tRNAs (P less than 5.10(-6). This correlation leads to the hypothesis that the process of hairpin unfolding can increase the time of translocation from the A to P ribosome site of the codon 5' to the hairpin, thus decreasing the probability of translational error (the latter would likely occur more frequently in the codons translated by minor tRNAs).

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Year:  1985        PMID: 3889832      PMCID: PMC340990          DOI: 10.1093/nar/13.1.275

Source DB:  PubMed          Journal:  Nucleic Acids Res        ISSN: 0305-1048            Impact factor:   16.971


  50 in total

1.  Studies on the bacteriophage MS2. Nucleotide fragments from the coat protein cistron.

Authors:  W M. Jou; G Haegeman; W Fiers
Journal:  FEBS Lett       Date:  1971-02-19       Impact factor: 4.124

2.  Mistranslation in E. coli.

Authors:  P Edelmann; J Gallant
Journal:  Cell       Date:  1977-01       Impact factor: 41.582

3.  Nucleotide sequence of the gene coding for the bacteriophage MS2 coat protein.

Authors:  W Min Jou; G Haegeman; M Ysebaert; W Fiers
Journal:  Nature       Date:  1972-05-12       Impact factor: 49.962

4.  The atp operon: nucleotide sequence of the promoter and the genes for the membrane proteins, and the delta subunit of Escherichia coli ATP-synthase.

Authors:  N J Gay; J E Walker
Journal:  Nucleic Acids Res       Date:  1981-08-25       Impact factor: 16.971

5.  The primary structure of E. coli RNA polymerase, Nucleotide sequence of the rpoC gene and amino acid sequence of the beta'-subunit.

Authors:  G S Monastyrskaya; V V Gubanov; S O Guryev; I S Salomatina; T M Shuvaeva; V M Lipkin; E D Sverdlov
Journal:  Nucleic Acids Res       Date:  1982-07-10       Impact factor: 16.971

6.  An energy model that predicts the correct folding of both the tRNA and the 5S RNA molecules.

Authors:  C Papanicolaou; M Gouy; J Ninio
Journal:  Nucleic Acids Res       Date:  1984-01-11       Impact factor: 16.971

7.  ampC cephalosporinase of Escherichia coli K-12 has a different evolutionary origin from that of beta-lactamases of the penicillinase type.

Authors:  B Jaurin; T Grundström
Journal:  Proc Natl Acad Sci U S A       Date:  1981-08       Impact factor: 11.205

8.  Translational accuracy in vitro.

Authors:  C G Kurland
Journal:  Cell       Date:  1982-02       Impact factor: 41.582

9.  Secondary structure of mRNA and efficiency of translation initiation.

Authors:  D Iserentant; W Fiers
Journal:  Gene       Date:  1980-04       Impact factor: 3.688

Review 10.  Preferential codon usage in prokaryotic genes: the optimal codon-anticodon interaction energy and the selective codon usage in efficiently expressed genes.

Authors:  H Grosjean; W Fiers
Journal:  Gene       Date:  1982-06       Impact factor: 3.688

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  13 in total

1.  Large-scale analysis of conserved rare codon clusters suggests an involvement in co-translational molecular recognition events.

Authors:  Matthieu Chartier; Francis Gaudreault; Rafael Najmanovich
Journal:  Bioinformatics       Date:  2012-03-30       Impact factor: 6.937

2.  Downstream secondary structure facilitates recognition of initiator codons by eukaryotic ribosomes.

Authors:  M Kozak
Journal:  Proc Natl Acad Sci U S A       Date:  1990-11       Impact factor: 11.205

3.  The genetic code is nearly optimal for allowing additional information within protein-coding sequences.

Authors:  Shalev Itzkovitz; Uri Alon
Journal:  Genome Res       Date:  2007-02-09       Impact factor: 9.043

4.  Nonuniform size distribution of nascent globin peptides, evidence for pause localization sites, and a contranslational protein-folding model.

Authors:  I A Krasheninnikov; A A Komar; I A Adzhubei
Journal:  J Protein Chem       Date:  1991-10

5.  Context effects and inefficient initiation at non-AUG codons in eucaryotic cell-free translation systems.

Authors:  M Kozak
Journal:  Mol Cell Biol       Date:  1989-11       Impact factor: 4.272

6.  Codon usage in histone gene families of higher eukaryotes reflects functional rather than phylogenetic relationships.

Authors:  D Wells; W Bains; L Kedes
Journal:  J Mol Evol       Date:  1986       Impact factor: 2.395

7.  Evolution of the IgA heavy chain gene in the genus Mus.

Authors:  B A Osborne; T E Golde; R L Schwartz; S Rudikoff
Journal:  Genetics       Date:  1988-08       Impact factor: 4.562

Review 8.  Errors and alternatives in reading the universal genetic code.

Authors:  J Parker
Journal:  Microbiol Rev       Date:  1989-09

9.  Ribosome-mediated translational pause and protein domain organization.

Authors:  T A Thanaraj; P Argos
Journal:  Protein Sci       Date:  1996-08       Impact factor: 6.725

10.  Synonymous codon usage influences the local protein structure observed.

Authors:  Rhodri Saunders; Charlotte M Deane
Journal:  Nucleic Acids Res       Date:  2010-06-08       Impact factor: 16.971

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