Student Work

Investigating the Unusual Gene Structure of DNA Primase in Mycobacteriophage Subclusters

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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.

  • 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.
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Identifier
  • E-project-042319-171703
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Year
  • 2019
Date created
  • 2019-04-23
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Permanent link to this page: https://digital.wpi.edu/show/nc580q656