Investigating the Unusual Gene Structure of DNA Primase in Mycobacteriophage SubclustersPublic
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In A4 and other subclusters of mycobacteriophages, DNA primase is a two-domain protein made from two genes with significant overlap that are read in different open reading frames. These genes create a functioning protein through an unknown mechanism. Our investigations using multiple sequence alignments and protein modelling do not support intein splicing, ribosomal frameshifting, or RNA polymerase slippage as mechanisms of forming a functional\nDNA primase. Preliminary RT-PCR results suggest both domains are transcribed on one transcript.
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