Faculty Advisor

Ryder, Elizabeth F.

Faculty Advisor

Whitefleet-Smith, JoAnn L.

Abstract

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.

Publisher

Worcester Polytechnic Institute

Date Accepted

April 2019

Major

Bioinformatics and Computational Biology

Major

Interdisciplinary

Project Type

Major Qualifying Project

Accessibility

Unrestricted

Advisor Department

Biology and Biotechnology

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