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

Examination of nascent globin peptides accumulating in vitro during globin synthesis in rabbit reticulocyte lysates was carried out. A view was supported that nonrandom distribution of codons with different usage frequencies in mRNA may determine the messenger's translation kinetics. Regions of reduced translation of alpha- and beta-globin polypeptide chains were localized, and the cotranslational protein-folding model suggested previously was substantiated. An active conjunction of synthesis and folding of proteins was proposed as one of the main destinations of a translation nonuniformity.