Literature DB >> 2742922

[Role of the code redundancy in determining cotranslational protein folding].

I A Krasheninnikov, A A Komar, I A Adzhubeĭ.   

Abstract

It has been demonstrated earlier in our laboratory that rare codon clusters can determine the boundaries of the polypeptide chain fragments of the same secondary structure type during the co-translational protein folding. According to this data, co-translational protein folding can occur under condition of a correlation between the frequency of codon choice in mRNAs and the relative abundance of their isoaccepting tRNAs. The alterations in the spectrum and concentrations of the isoaccepting tRNAs in different cells were demonstrated by many authors. The existence of a mechanism of the coordinate regulation of the levels (activities) of the isoaccepting tRNAs, corresponding aminoacyl-tRNA synthetases and mRNAs predominantly translated at a given moment of time can be suggested. Such a mechanism can ensure the needed accuracy of the protein folding process. Analysis of gene sequences of various pro- and eukaryotic organisms carried out in the present work revealed that the codon usage frequency spectra of simultaneously synthesized proteins are similar. The relative appearance of the most rare and frequent codons in investigated gene sequences displays a high degree of conservatism. It has also been found that structural-homologous proteins from different organisms (cytochromes c, myoglobins) have very similar codon frequency distribution profiles. This property retains despite the significant variations in the codon usage spectra in the investigated gene sequences. The data obtained indicate that the codon distribution in mRNAs whose diversity is mainly conditioned by the genetic code redundance is a program that determines translational rates of different mRNA parts thus controlling the spatial folding of the synthesized peptide chain.

Mesh:

Substances:

Year:  1989        PMID: 2742922

Source DB:  PubMed          Journal:  Biokhimiia        ISSN: 0320-9725


  8 in total

1.  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

2.  Protein secondary structural types are differentially coded on messenger RNA.

Authors:  T A Thanaraj; P Argos
Journal:  Protein Sci       Date:  1996-10       Impact factor: 6.725

3.  Network analysis of synonymous codon usage.

Authors:  Khalique Newaz; Gabriel Wright; Jacob Piland; Jun Li; Patricia L Clark; Scott J Emrich; Tijana Milenković
Journal:  Bioinformatics       Date:  2020-12-08       Impact factor: 6.937

4.  An Integrated Sequence-Structure Database incorporating matching mRNA sequence, amino acid sequence and protein three-dimensional structure data.

Authors:  I A Adzhubei; A A Adzhubei; S Neidle
Journal:  Nucleic Acids Res       Date:  1998-01-01       Impact factor: 16.971

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

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

Review 6.  Birth, life and death of nascent polypeptide chains.

Authors:  Sujata Jha; Anton A Komar
Journal:  Biotechnol J       Date:  2011-04-29       Impact factor: 4.677

Review 7.  Genetic code redundancy and its influence on the encoded polypeptides.

Authors:  Paige S Spencer; José M Barral
Journal:  Comput Struct Biotechnol J       Date:  2012-03-20       Impact factor: 7.271

8.  Generic algorithm to predict the speed of translational elongation: implications for protein biogenesis.

Authors:  Gong Zhang; Zoya Ignatova
Journal:  PLoS One       Date:  2009-04-03       Impact factor: 3.240

  8 in total

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