Coding nucleic acids are chaperons for protein folding: a novel theory of protein folding

Gene. 2013 Feb 25;515(2):249-57. doi: 10.1016/j.gene.2012.12.048. Epub 2012 Dec 20.

Abstract

The arguments for nucleic acid chaperons are reviewed and three new lines of evidence are added. (1) It was found that amino acids encoded by codons in short nucleic acid loops frequently form turns and helices in the corresponding protein structures. (2) The amino acids encoded by partially complementary (1st and 3rd nucleotides) codons are more frequently co-located in the encoded proteins than expected by chance. (3) There are significant correlations between thermodynamic changes (ddG) caused by codon mutations in nucleic acids and the thermodynamic changes caused by the corresponding amino acid mutations in the encoded proteins. We conclude that the concept of the Proteomic Code and nucleic acid chaperons seems correct from the bioinformatics point of view, and we expect to see direct biochemical experiments and evidence in the near future.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Base Sequence
  • Codon
  • Computer Simulation*
  • DNA, Complementary / chemistry
  • DNA, Complementary / genetics
  • Models, Molecular*
  • Molecular Sequence Data
  • Mutation
  • Nucleic Acid Conformation
  • Open Reading Frames*
  • Protein Folding*
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Proteins / chemistry
  • Proteins / genetics
  • RNA, Messenger / chemistry
  • RNA, Messenger / genetics
  • Sequence Analysis, DNA
  • Thermodynamics

Substances

  • Codon
  • DNA, Complementary
  • Proteins
  • RNA, Messenger