Proteomic code

On the basis of recent fundamentally novel developments in the protein structure a proteomic code is suggested, that would potentially allow to describe sequence, structure, and function of proteins by a spectrum of elementary loop-n-lock units. All major characteristics of the nearly standard units are described, and first five "codons" of the proteomic code are presented with their respective unique sequences, structures, and functions. More such codons are to be discovered, and the general procedure for their identification is described.     

The genetic code, an instantaneous absolutely optimal code

The genetic code is an instantaneous code i.e., each codon is deciphered out of ambiguities without knowing other symbols than the constituting nucleotides. Moreover entropy of the genetic source of information has a maximal value.     

A code within a code: how codons influence mRNA stability

The genetic code was deciphered more than 50 years ago, but we are only now becoming aware of a second, hidden code. It is the concept of “codon optimality” that enters the scene of developmental and homeostatic gene expression, linking translation rates, mRNA stability, and tRNA abundance. Both at the biological and methodological levels, work by Giraldez and colleagues in this issue of The EMBO Journal paves the way for further analyses of such key regulatory mechanisms.     

Evolutionary roots of genetic code

It is presented the modern state of the problem on abiogenic synthesis of molecular mechanisms connected with genetic information storage and transfer. On the base of experimental results it is suggested model of the common ancestor of tRNA and prime mechanism of the specific peptide synthesis.     

Mistranslation of the genetic code

During mRNA decoding at the ribosome, deviations from stringent codon identity, or “mistranslation,” are generally deleterious and infrequent. Observations of organisms that decode some codons ambiguously, and the discovery of a compensatory increase in mistranslation frequency to combat environmental stress have changed the way we view “errors” in decoding. Modern tools for the study of the frequency and phenotypic effects of mistranslation can provide quantitative and sensitive measurements of decoding errors that were previously inaccessible. Mistranslation with non-protein amino acids, in particular, is an enticing prospect for new drug therapies and the study of molecular evolution.