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.

• This report represents the work of one or more WPI undergraduate students submitted to the faculty as evidence of completion of a degree requirement. WPI routinely publishes these reports on its website without editorial or peer review.

Creator

• Champlin, Daniel Mathieu
• Payano, Jennifer A.
• O'Connell, Eoin J.

Publisher

• Worcester Polytechnic Institute

Identifier

• E-project-042319-171703

Advisor

• Ryder, Elizabeth F.
• Whitefleet-Smith, JoAnn L.

Year

• 2019

Date created

• 2019-04-23

Resource type

• Major Qualifying Project

Major

• Bioinformatics & Computational Biology
• Interdisciplinary

Rights statement

• In Copyright

License

• All rights reserved