Induction of eIF‐4E phosphorylation by the addition of L‐pyrroline‐5‐carboxylic acid to rabbit reticulocyte lysate

Abstract
Addition of L‐pyrroline‐5‐carboxylic acid to reticulocyte lysates inhibits protein synthesis and induced phosphoproteins of 25 and 14 kDa. The 25 kDa phosphoprotein had the same M r and pI as phosphorylated eIF‐4E. Incubation of lysates with L‐pyrroline‐5‐carboxylic acid did not alter the crosslinking of eIF‐4E to reovirus mRNA caps. These results suggest that modifications of the translational apparatus other than eIF‐4E phosphorylation may mediate the inhibitory effect seen with L‐pyrroline‐5‐carboxylic acid and/or that phosphorylation of eIF‐4E may effect functions subsequent to its interaction with the mRNA cap such as protein‐protein interactions with other cap‐specific translation factors.

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