Protein secondary structural types are differentially coded on messenger RNA

Research output: Contribution to journalArticlepeer-review

131 Citations (Scopus)

Abstract

Tricodon regions on messenger RNAs corresponding to a set of proteins from Escherichia coli were scrutinized for their translation speed. The fractional frequency values of the individual codons as they occur in mRNAs of highly expressed genes from Escherichia coli were taken as an indicative measure of the translation speed. The tricodons were classified by the sum of the frequency values of the constituent codons. Examination of the conformation of the encoded amino acid residues in the corresponding protein tertiary structures revealed a correlation between codon usage in mRNA and topological features of the encoded proteins. Alpha helices on proteins tend to be preferentially coded by translationally fast mRNA regions while the slow segments often code for beta strands and coil regions. Fast regions correspondingly avoid coding for beta strands and coil regions while the slow regions similarly move away from encoding alpha helices. Structural and mechanistic aspects of the ribosome peptide channel support the relevance of sequence fragment translation and subsequent conformation. A discussion is presented relating the observation to the reported kinetic data on the formation and stabilization of protein secondary structural types during protein folding. The observed absence of such strong positive selection for codons in non highly expressed genes is compatible with existing theories that mutation pressure may well dominate codon selection in non highly expressed genes.

Original languageEnglish
Pages (from-to)1973-1983
Number of pages11
JournalProtein Science
Volume5
Issue number10
DOIs
Publication statusPublished - 1 Jan 1996

Keywords

  • alpha helices
  • beta strands
  • codon usage
  • coils
  • protein folding
  • translation speed

Fingerprint Dive into the research topics of 'Protein secondary structural types are differentially coded on messenger RNA'. Together they form a unique fingerprint.

Cite this