Abstract

Unique peptide sequences often direct protein localization to specific cellular sites. However, on-site translation of mRNAs also provides an efficient means of subcellular protein localization. Katsafanas and Moss (e01671-19) found that on-site translation occurred for the poxvirus mRNA that encodes the 150-kDa A-type inclusion (ATI) protein, which forms large inclusion bodies that sequester viral particles. Nascent peptides anchored ATI mRNA at the inclusions, permitting multiple rounds of translation and thereby preventing premature protein aggregation and trapping of virions at transcription sites. These findings shed light on the coordination of transcription, translation, and virion assembly during the poxvirus life cycle.

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