Ryder, Elizabeth F.
Whitefleet-Smith, JoAnn L.
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 DNA primase. Preliminary RT-PCR results suggest both domains are transcribed on one transcript.
Worcester Polytechnic Institute
Bioinformatics and Computational Biology
Major Qualifying Project
All authors have granted to WPI a nonexclusive royalty-free license to distribute copies of the work, subject to other agreements. Copyright is held by the author or authors, with all rights reserved, unless otherwise noted.
Biology and Biotechnology