Selective inhibition of proteins synthesized from different mRNA species in reticulocyte lysates containing L-pyrroline-5-carboxylic acid.

L-Pyrroline-5-carboxylic acid is a naturally occurring nonprotein amino acid present in human plasma that changes concentrations with diet. L-pyrroline-5-carboxylic acid inhibited net synthesis of globin in untreated reticulocyte lysates in a dose dependent manner. This inhibition was greater than that observed with equimolar GSSG or NADP+ and was prevented by a NADPH generating system. L-pyrroline-5-carboxylic acid also inhibited net synthesis of proteins from brome mosaic and alfalfa mosaic virus mRNAs to different extents. However, no effect on the translation of the naturally uncapped encephalomyocarditis virus mRNA was observed. In general, mRNAs that are considered strongly competitive, such as alfalfa mosaic virus 2 and 4, were more resistant to this inhibitory process. These results indicate that pyrroline-5-carboxylic acid can initiate a differential effect on proteins synthesized from different mRNA species by an as yet unidentified mechanism.